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Genomes and Genes
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| Ivano BertiniSummaryCountry: Italy Publications
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Publications
Conformational variability of matrix metalloproteinases: beyond a single 3D structureIvano Bertini
Magnetic Resonance Center Centro di Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 102:5334-9. 2005..Backbone flexibility may play a role in the difficulties encountered in the design of selective inhibitors, whereas it may be a requisite for substrate binding and broad substrate specificity...
A NMR study of the interaction of a three-domain construct of ATP7A with copper(I) and copper(I)-HAH1: the interplay of domainsLucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Chem 280:38259-63. 2005..This dependence could constitute the molecular mechanism to trigger copper(I) translocation and/or ATP7A relocalization from the trans-Golgi network to the plasmatic membrane...
Structural basis for the function of the N-terminal domain of the ATPase CopA from Bacillus subtilisLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Biol Chem 278:50506-13. 2003....
Solution structure of Cox11, a novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidaseLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino 50019, Florence, Italy
J Biol Chem 279:34833-9. 2004..The present results advance the knowledge on the poorly understood molecular aspects of cytochrome c oxidase assembly...
Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1Lucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 46:9953-62. 2007..These results suggest further that it is the metal-free apo forms of the mutant SOD1 protein that are the agents of its toxicity...
Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solutionLucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Chem 280:35815-21. 2005..We have here also established that the two free cysteines (6 and 111) do not play a role in this behavior...
A prokaryotic superoxide dismutase paralog lacking two Cu ligands: from largely unstructured in solution to ordered in the crystalLucia Banci
Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto, Florence, Italy
Proc Natl Acad Sci U S A 102:7541-6. 2005..Couples of dimers held by hydrophobic interactions and H bonds are further organized in long chains. The order/disorder transition is discussed in terms of metal binding and physical state...
Protein stability and mutations in the axial methionine loop of a minimal cytochrome cIlaria Bartalesi
Magnetic Resonance Center, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Inorg Chem 9:600-8. 2004..While the structure remains essentially the same, the stability decreases with mutations. The comparison with mitochondrial c-type cytochromes is instructive...
Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domainsIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Am Chem Soc 129:12786-94. 2007..Such variety is somewhat reduced in the calmodulin-alpha-synuclein adduct, which however still retains high flexibility. The flexibility of the calmodulin-alpha-synuclein adduct is an unexpected result of this research...
Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7ALucia Banci
Magnetic Resonance Center, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 43:3396-403. 2004..A comparison with metallochaperones and soluble domains of P-type ATPases allows us to relate the primary structure to the occurrence of structural rearrangements upon copper binding...
Understanding copper trafficking in bacteria: interaction between the copper transport protein CopZ and the N-terminal domain of the copper ATPase CopA from Bacillus subtilisLucia Banci
Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino Florence, Italy
Biochemistry 42:1939-49. 2003..Comparing functional data of homologous proteins of other bacteria, it can be concluded that this class of proteins is involved in copper homeostasis but the specific roles are species dependent...
NMR structural analysis of cadmium sensing by winged helix repressor CmtRLucia Banci
Department of Chemistry and Centro Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, Florence 50019, Italy
J Biol Chem 282:30181-8. 2007..Cadmium binding across the dimer interface impairs DNA association by excluding the apo-conformers suited to bind DNA...
From an inactive prokaryotic SOD homologue to an active protein through site-directed mutagenesisLucia Banci
Department of Chemistry and Centro Risonanze Magnetiche, University of Florence, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 127:13287-92. 2005..The catalytic properties of the double mutant, which might be regarded as a step in an artificial evolution from a nonactive SOD to a fully functioning enzyme, are discussed on the basis of the structural and dynamical properties...
Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1Lucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochem Biophys Res Commun 364:645-9. 2007..Similar results are found in ATPases from other organisms and may represent a general feature, whose biochemical implications are not yet fully appreciated...
Solution structure of Apo Cu,Zn superoxide dismutase: role of metal ions in protein foldingLucia Banci
Department of Chemistry and Centro Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 42:9543-53. 2003....
The evolutionarily conserved trimeric structure of CutA1 proteins suggests a role in signal transductionFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Biol Chem 278:45999-6006. 2003..This similarity suggests an intriguing role of CutA1 proteins in signal transduction through allosteric communications between subunits...
Solution structure of apo CopZ from Bacillus subtilis: further analysis of the changes associated with the presence of copperLucia Banci
Department of Chemistry and Centro di Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
Biochemistry 42:13422-8. 2003..It is also shown that copper(I) exchanges among apo CopZ molecules in slow exchange on the NMR time scale, whereas it is known that such exchange between partner molecules (i.e., metallochaperones and metal pumps) is fast...
The Atx1-Ccc2 complex is a metal-mediated protein-protein interactionLucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Nat Chem Biol 2:367-8. 2006..Copper was required for the interaction. This study provides an understanding of metal-mediated protein-protein interactions in which the metal ion is essential for the weak, reversible interaction between the partners...
SOD1 and amyotrophic lateral sclerosis: mutations and oligomerizationLucia Banci
Magnetic Resonance Center CERM, Department of Chemistry, University of Florence, Florence, Italy
PLoS ONE 3:e1677. 2008..The mechanism here proposed for SOD1 mutant oligomerization is absolutely general and it provides a common unique picture for the behaviors of the many SOD1 mutants, of different nature and distributed all over the protein...
Mitochondrial copper(I) transfer from Cox17 to Sco1 is coupled to electron transferLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
Proc Natl Acad Sci U S A 105:6803-8. 2008....
Solution structures of the actuator domain of ATP7A and ATP7B, the Menkes and Wilson disease proteinsLucia Banci
Magnetic Resonance Center CERM University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 48:7849-55. 2009....
NMR structural analysis of the soluble domain of ZiaA-ATPase and the basis of selective interactions with copper metallochaperone Atx1Lucia Banci
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
J Biol Inorg Chem 15:87-98. 2010..These few residues of the two ATPases have diverged during evolution to bias Atx1 interactions in favor of PacS(N) rather than ZiaA(N.)...
Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS)Lucia Banci
Magnetic Resonance Center, University of Florence, 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 109:13555-60. 2012..Domain 3 is responsible for the catalytic formation of the hSOD1 Cys-57-Cys-146 disulfide bond, which involves both hCCS Cys-244 and Cys-246 via disulfide transfer...
A structural-dynamical characterization of human Cox17Lucia Banci
Magnetic Resonance Center Centro Risonanze Magnetiche CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Biol Chem 283:7912-20. 2008..The copper(I) form of Cox17(2S-S) has features specific for copper chaperones...
The different intermolecular interactions of the soluble copper-binding domains of the menkes protein, ATP7ALucia Banci
Magnetic Resonance Center, Via L Sacconi 6, and Department of Chemistry, Via della Lastruccia 3, University of Florence, Italy
J Biol Chem 282:23140-6. 2007....
Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfacesLucia Banci
Magnetic Resonance Center CERM, University of Florence, Sesto Fiorentino, Italy
Biochem J 422:37-42. 2009..It appears that electrostatics is important in selecting which domain of the ATPase is able to form detectable amounts of the metal-mediated adduct with HAH1...
Solution structure and dynamics of S100A5 in the apo and Ca2+-bound statesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Inorg Chem 14:1097-107. 2009....
Human SOD1 before harboring the catalytic metal: solution structure of copper-depleted, disulfide-reduced formLucia Banci
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Biol Chem 281:2333-7. 2006..The structure allows us to further discuss the copper loading mechanism in SOD1...
Superoxide dismutase folding/unfolding pathway: role of the metal ions in modulating structural and dynamical featuresMichael Assfalg
CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Mol Biol 330:145-58. 2003..4 M, thus demonstrating the importance of metal ions with respect to the unfolding process and protein structure stability. Hints to understand the whole folding process are obtained and discussed...
Structural insights into the ferroxidase site of ferritins from higher eukaryotesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, 50019 Sesto Fiorentino, Florence, Italy
J Am Chem Soc 134:6169-76. 2012..Here two different di-iron species are trapped in the active site, with intermetal distances corresponding to those of the ferric dimer in crystal 1 and of the dicopper centers and corresponding rearrangement of the His54 side chain...
In-cell NMR in E. coli to monitor maturation steps of hSOD1Lucia Banci
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
PLoS ONE 6:e23561. 2011..However, no intramolecular disulfide bridge formation occurs, nor copper uptake, suggesting the need of a specific chaperone for those purposes...
An atomic-level investigation of the disease-causing A629P mutant of the Menkes protein, ATP7ALucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Mol Biol 352:409-17. 2005..A small reduction of the affinity for copper(I) is also observed. Both effects could concur to pathogenicity...
Structural interplay between calcium(II) and copper(II) binding to S100A13 proteinFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 44:6341-4. 2005
Structural and dynamic aspects related to oligomerization of apo SOD1 and its mutantsLucia Banci
Magnetic Resonance Center and Department of Chemistry, Fiorgen Foundation, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 106:6980-5. 2009..The present results suggest that the investigation of the solution state coupled with that of the crystal state can provide major insights into SOD1 pathway toward oligomerization in relation to fALS...
15N-1H Residual dipolar coupling analysis of native and alkaline-K79A Saccharomyces cerevisiae cytochrome cMichael Assfalg
Magnetic Resonance Center (CERM, University of Florence, 50019 Sesto Fiorentino, Florence, Italy
Biophys J 84:3917-23. 2003..Importantly, this is the first time that mobility has been found through comparison of RDCs with pseudocontact shifts...
Ortholog search of proteins involved in copper delivery to cytochrome C oxidase and functional analysis of paralogs and gene neighbors by genomic contextFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
J Proteome Res 4:63-70. 2005..By linking the assembly system to the copper uptake system, Sco allows COX to face alternative copper trafficking pathways...
A strategy for the NMR characterization of type II copper(II) proteins: the case of the copper trafficking protein CopC from Pseudomonas SyringaeFabio Arnesano
CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Am Chem Soc 125:7200-8. 2003..The knowledge of the location of the Cu(II) in the protein is important for the copper transfer mechanism...
Solution structures of a cyanobacterial metallochaperone: insight into an atypical copper-binding motifLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Biol Chem 279:27502-10. 2004....
X-ray absorption and NMR spectroscopic studies of CopZ, a copper chaperone in Bacillus subtilis: the coordination properties of the copper ionLucia Banci
Centro di Risonanze Magnetiche and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
Biochemistry 42:2467-74. 2003..These results are instructive and have been discussed with respect to the molecular basis of copper trafficking...
Combining in silico tools and NMR data to validate protein-ligand structural models: application to matrix metalloproteinasesIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Med Chem 48:7544-59. 2005..This protocol is proposed as a viable alternative to the many approaches described in the literature...
Structural basis for metal binding specificity: the N-terminal cadmium binding domain of the P1-type ATPase CadALucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Mol Biol 356:638-50. 2006....
The binding mode of ATP revealed by the solution structure of the N-domain of human ATP7ALucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Italy
J Biol Chem 285:2537-44. 2010....
Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machineryLucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
Chem Biol 18:794-804. 2011..Hence, anamorsin is the first identified Fe/S protein imported into the IMS, raising the possibility that it plays a role in cytosolic Fe/S cluster biogenesis also once trapped in the IMS...
An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALRLucia Banci
Magnetic Resonance Center, University of Florence, Via L Sacconi 6, Sesto Fiorentino, Italy
J Am Chem Soc 134:1442-5. 2012..This finding allows us to present a complete model for the electron-transfer pathway in ALR...
Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper bindingFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Sesto Fiorentino, Florence 50019, Italy
Structure 13:713-22. 2005..This form of the protein is oligomeric. These properties are framed within a complete model of mitochondrial import and COX assembly...
Solution structure and intermolecular interactions of the third metal-binding domain of ATP7A, the Menkes disease proteinLucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Chem 281:29141-7. 2006..Copper(I) transfer from metal-loaded HAH1 was observed experimentally, but the metal distribution was shifted toward binding by HAH1. This is at variance with what is observed for the other Menkes domains...
Metal binding domains 3 and 4 of the Wilson disease protein: solution structure and interaction with the copper(I) chaperone HAH1Lucia Banci
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 47:7423-9. 2008..The ability of HAH1 to form a complex only with some domains of ATP7B is an interesting property of this class of proteins and may have a signaling role in the function of the ATPases...
Solution structure of Sco1: a thioredoxin-like protein Involved in cytochrome c oxidase assemblyErica Balatri
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
Structure 11:1431-43. 2003..The availability of the structure has allowed us to model the homologs Sco1 and Sco2 from S. cerevisiae and to discuss the physiological role of the Sco family...
Structure and dynamics of reduced Bacillus pasteurii cytochrome c: oxidation state dependent properties and implications for electron transfer processesIlaria Bartalesi
Centro di Risonanze Magnetiche, University of Florence, Sesto Fiorentino, Italy
Biochemistry 42:739-45. 2003..By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes...
Solution structure and characterization of the heme chaperone CcmEFabio Arnesano
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
Biochemistry 41:13587-94. 2002..The data available suggest that the heme transfer process is likely to involve a heterooligomeric protein complex and occur under a tight enzymatic control...
Solid-state NMR of matrix metalloproteinase 12: an approach complementary to solution NMRStéphane Balayssac
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Chembiochem 8:486-9. 2007
A core mutation affecting the folding properties of a soluble domain of the ATPase protein CopA from Bacillus subtilisLucia Banci
Department of Chemistry, The Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Mol Biol 331:473-84. 2003..This study contributes to understanding the behaviour of proteins that do not properly fold in vitro. A possible biological significance of the peculiar folding behaviour of this domain is discussed...
The unfolding of oxidized c-type cytochromes: the instructive case of Bacillus pasteuriiIlaria Bartalesi
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Mol Biol 321:693-701. 2002..It is concluded that the thermodynamic stability of the region around the metal cofactor is determined by the chemical nature of the residues around the axial methionine residue...
Paramagnetism-based refinement strategy for the solution structure of human alpha-parvalbuminIrfan Baig
Magnetic Resonance Centre and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 43:5562-73. 2004..0 A resolution. All differences are related to local changes in the amino acidic composition...
Affinity gradients drive copper to cellular destinationsLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
Nature 465:645-8. 2010..Our study provides the thermodynamic basis for the kinetic processes that lead to the distribution of cellular copper...
Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examplesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 131:5134-44. 2009....
Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1)Ivano Bertini
Magnetic Resonance Center, University of Florence, Sesto Fiorentino, Italy
J Biol Chem 284:12821-8. 2009....
Occurrence of copper proteins through the three domains of life: a bioinformatic approachClaudia Andreini
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Proteome Res 7:209-16. 2008..A network involving proteins having roles in both copper transport and respiration was identified, parts or all of which are detected in the majority of the organisms examined...
A structural characterization of human SCO2Lucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
Structure 15:1132-40. 2007..Such differences are accounted for in terms of the different physicochemical properties in strategic protein locations. The misfunction of the known pathogenic mutations is discussed on the basis of the obtained structure...
The delivery of copper for thylakoid import observed by NMRLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
Proc Natl Acad Sci U S A 103:8320-5. 2006..Contact with PacS(N) induces change to the ScAtx1 copper-coordination sphere that drives copper release for thylakoid import. These data also elaborate on the mechanism to keep copper(I) out of the ZiaA(N) ATPase zinc sites...
Copper proteomes, phylogenetics and evolutionLeonardo Decaria
Magnetic Resonance Center CERM University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Metallomics 3:56-60. 2011..It is shown that evolution is a coordinated development of the chemistry of elements with use of novel and multiple copies of their proteins as their availability rises in the environment...
Exploring the subtleties of drug-receptor interactions: the case of matrix metalloproteinasesIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 129:2466-75. 2007....
The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide statusFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Biol Chem 279:47998-8003. 2004..This finding provides a basis for understanding the selectivity of mitochondrial SOD1 import and may be relevant to the toxic properties of mutant forms of hSOD1 that can cause the familial form of amyotrophic lateral sclerosis...
Mapping protein-protein interaction by 13C'-detected heteronuclear NMR spectroscopyIvano Bertini
Department of Chemistry, University of Florence, 50019, Sesto Fiorentino, Italy
J Biomol NMR 36:111-22. 2006..It is here proposed that protonless (13)C direct-detection NMR is a useful complement to (1)H based NMR spectroscopy for monitoring protein-protein and protein-ligand interactions...
Solution structure of a monoheme ferrocytochrome c from Shewanella putrefaciens and structural analysis of sequence-similar proteins: functional implicationsIlaria Bartalesi
Centro di Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 41:5112-9. 2002..The structures of the others have been modeled by using the available templates and internally validated. Structural similarities in terms of surface properties account for their biophysical features and provide hints about the function...
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitorsLuis A Alcaraz
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, Sesto Fiorentino, Italy
J Biol Inorg Chem 12:1197-206. 2007....
Evidence of reciprocal reorientation of the catalytic and hemopexin-like domains of full-length MMP-12Ivano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Am Chem Soc 130:7011-21. 2008..Hints on the probable conformations are also obtained. This experimental finding opens new perspectives for the often hypothesized active role of the hemopexin-like domain in the enzymatic activity of MMPs...
Ultrafast MAS solid-state NMR permits extensive 13C and 1H detection in paramagnetic metalloproteinsIvano Bertini
Magnetic Resonance Center, CERM, University of Florence, Sesto Fiorentino, Italy
J Am Chem Soc 132:5558-9. 2010..Furthermore, using the known crystal structure of the compound, we are able to distinguish and measure pseudocontact (PCS) contributions to the shifts up to the coordinating ligands and to unveil structural information...
A use of Ramachandran potentials in protein solution structure determinationsIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Biomol NMR 26:355-66. 2003..The quality of the structures, and of Ramachandran plot statistics in particular, was notably improved while preserving the agreement with the experimental constraints...
X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinasesIvano Bertini
Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi, 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 42:2673-6. 2003
Cross correlation rates between Curie spin and dipole-dipole relaxation in paramagnetic proteins: the case of cerium substituted calbindin D9kIvano Bertini
Magnetic Resonance Center, University of Florence, Italy
J Biomol NMR 23:115-25. 2002..This integrated structure calculation protocol has the advantage that different paramagnetic-based constraints are treated by the same algorithm in a way that the efficiency of each class of constraints can be analyzed and compared...
NMR-validated structural model for oxidized Rhodopseudomonas palustris cytochrome c(556)Ivano Bertini
CERM and Department of Chemistry, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
J Biol Inorg Chem 9:224-30. 2004..The directions and magnitude of the magnetic susceptibility anisotropy tensor were also calculated. The approach readily provides useful results, especially for paramagnetic metalloproteins of moderate to large dimensions...
Structural model for an alkaline form of ferricytochrome CMichael Assfalg
CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Am Chem Soc 125:2913-22. 2003..Based on several spectral features, we conclude that the folded polypeptide is highly fluxional...
A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118)Lucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Mol Biol 323:883-97. 2002....
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondriaLucia Banci
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Florence, Italy
Nat Struct Mol Biol 16:198-206. 2009..MIA40 represents a thioredoxin-unrelated, minimal oxidoreductase, with a facile CPC redox active site that ensures its catalytic function in oxidative folding in mitochondria...
Paramagnetically induced residual dipolar couplings for solution structure determination of lanthanide binding proteinsRenato Barbieri
Magnetic Resonance Center and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Am Chem Soc 124:5581-7. 2002..The effect of mobility is also assessed. In principle, information on the mobility can be obtained with a number of lanthanide ions >5, or by combining a smaller number of lanthanide ions with a few orienting devices...
Tuning the affinity for lanthanides of calcium binding proteinsIvano Bertini
Magnetic Resonance Center and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
Biochemistry 42:8011-21. 2003..Finally, by using CaM samples containing only three of the four calcium ions, it was possible to prepare well-defined Ca(3)Ln-CaM derivatives (Ln = Tb, Dy, Tm, and Yb), with interesting properties as NMR probes...
Solution structure of CopC: a cupredoxin-like protein involved in copper homeostasisFabio Arnesano
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Sesto Fiorentino, Florence, Italy
Structure 10:1337-47. 2002..The present structure represents a link between copper-trafficking proteins and cupredoxins. Within a structural and genomic analysis, the role of CopC in copper trafficking is discussed...
A high-resolution NMR study of long-lived water molecules in both oxidation states of a minimal cytochrome cIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 42:3457-63. 2003....
Application of NMRD to hydration of rubredoxin and a variant containing a (Cys-S)3FeIII(OH) siteIvano Bertini
CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biophys J 84:545-51. 2003..1)H nuclear magnetic relaxation dispersion profiles indicate increased hydration with respect to the wild-type...
Intra- and interdomain flexibility in matrix metalloproteinases: functional aspects and drug designIvano Bertini
Magnetic Resonance Center CERM, University of Florence, Via L Sacconi 6, 50019 Sesto Fiorentino, Italy
Curr Pharm Des 15:3592-605. 2009..The implications of the observed intra- and interdomain flexibility in matrix metalloproteinases for drug design have been analyzed and discussed...
NMR spectroscopy of paramagnetic metalloproteinsIvano Bertini
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Chembiochem 6:1536-49. 2005..Finally, a section is dedicated to the significant progress made on 13C direct detection, which reduces the negative effects of paramagnetism and may constitute a new chapter in the whole field of NMR spectroscopy...
Comparative analysis of the ADAM and ADAMTS familiesClaudia Andreini
Magnetic Resonance Center (CERM, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
J Proteome Res 4:881-8. 2005....
A quick solution structure determination of the fully oxidized double mutant K9-10A cytochrome c7 from Desulfuromonas acetoxidans and mechanistic implicationsMichael Assfalg
Magnetic Resonance Center and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
J Biomol NMR 22:107-22. 2002..This finding is in agreement with the identification of the protein area around heme IV as the interacting site...
A 15N NMR mobility study on the dicalcium P43M calbindin D9k and its mono-La3+-substituted formIvano Bertini
Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
Biochemistry 41:5104-11. 2002..They also demonstrate that substitution of a lanthanide ion for calcium, which is a common procedure, does not significantly alter the mobility of the native protein...
Backbone-only restraints for fast determination of the protein fold: the role of paramagnetism-based restraints. Cytochrome b562 as an exampleLucia Banci
CERM and Department of Chemistry, University of Florence, Sesto Fiorentino, Italy
J Magn Reson 172:191-200. 2005..The paramagnetism based restraints are shown to be absolutely relevant, especially for Deltardc's...
NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteriaLucia Banci
Centro di Risonanze Magnetiche, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Chembiochem 3:299-310. 2002..At variance with mitochondrial c-type cytochrome, this protein does not experience pH-dependent coordination equilibria. The reasons for this difference are analyzed...
The solution structure of reduced dimeric copper zinc superoxide dismutase. The structural effects of dimerizationLucia Banci
Department of Chemistry and Centro Risonanze Magnetiche, University of Florence, Italy
Eur J Biochem 269:1905-15. 2002..Finally, the conformation of the key Arg143 residue is compared to that in the other dimeric and monomeric structures as well as in the recently reported structure of the CCS-superoxide dismutase (SOD) complex...
Integration of XAS and NMR techniques for the structure determination of metalloproteins. Examples from the study of copper transport proteinsLucia Banci
Magnetic Resonance Center (CERM) and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy
J Synchrotron Radiat 12:94-7. 2005..The synergism of the two techniques has been exploited in the structure determination of bacterial copper transport proteins...
High-resolution solid-state NMR structure of a 17.6 kDa proteinIvano Bertini
Magnetic Resonance Center, CERM, University of Florence, Via L Sacconi, 6 50019 Sesto Fiorentino, Italy
J Am Chem Soc 132:1032-40. 2010..3 A). The proposed strategy, which may be generalized for nonmetalloproteins with the use of paramagnetic tags, represents a significant step ahead in protein structure determination using solid-state NMR...
Cytochrome c and organic molecules: solution structure of the p-aminophenol adductMichael Assfalg
ProtEra srl, Viale delle Idee 22, 50019 Sesto Fiorentino, Italy
Biochemistry 46:6232-8. 2007..Small but meaningful rearrangements of the solvent-exposed side chains are observed upon ligand binding and contribute to the stabilization of the complex...
NMR reveals pathway for ferric mineral precursors to the central cavity of ferritinPaola Turano
Department of Chemistry, University of Florence, Magnetic Resonance Center, 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 107:545-50. 2010..Multiple iron channel exits are near enough to facilitate high concentration of iron that can mineralize in the ferritin cavity, illustrating advantages of the multisubunit cage structure...
Dynamic properties of the G93A mutant of copper-zinc superoxide dismutase as detected by NMR spectroscopy: implications for the pathology of familial amyotrophic lateral sclerosisEric L Shipp
Magnetic Resonance Center CERM, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Biochemistry 42:1890-9. 2003..Alternatively, a motor neuron-specific substrate may bind this region of the protein, leading to deleterious modifications and/or reactions...
Solution structure of the N-terminal domain of a potential copper-translocating P-type ATPase from Bacillus subtilis in the apo and Cu(I) loaded statesLucia Banci
Magnetic Resonance Center CERM and Department of Chemistry, University of Florence, Via Luigi Sacconi 6, Florence, Sesto Fiorentino, 50019, Italy
J Mol Biol 317:415-29. 2002....
Browsing gene banks for Fe2S2 ferredoxins and structural modeling of 88 plant-type sequences: an analysis of fold and functionIvano Bertini
Centro di Risonanze Magnetiche, University of Florence, Sesto Fiorentino, Italy
Proteins 46:110-27. 2002....
An NMR study of the interaction between the human copper(I) chaperone and the second and fifth metal-binding domains of the Menkes proteinLucia Banci
Magnetic Resonance Center CERM, University of Florence, Italy
FEBS J 272:865-71. 2005..The results are discussed in comparison with the data available in the literature for the interaction between HAH1 and its partners from other spectroscopic techniques...
Paramagnetic metal ions in ligand screening: the Co(II) matrix metalloproteinase 12Ivano Bertini
Magnetic Resonance Center, University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino, Italy
Angew Chem Int Ed Engl 43:2254-6. 2004
Paramagnetism-based restraints for Xplor-NIHLucia Banci
CERM and Department of Chemistry, University of Florence, Via L. Sacconi, 6, I-50019 Sesto Fiorentino, Italy
J Biomol NMR 28:249-61. 2004..The agreement between the two programs is quite satisfactory and validates both protocols...
A further investigation of the cytochrome b5-cytochrome c complexLucia Banci
Magnetic Resonance Center (CERM, University of Florence, Via Luigi Sacconi 6, 50019, Sesto Fiorentino, Italy
J Biol Inorg Chem 8:777-86. 2003..All the species are in fast exchange on the scale of differences in chemical shift. By comparison with literature data, it appears that the structure of one 1:1 adduct changes with the origin or primary sequence of cytochrome b(5)...
The magnetic properties of myoglobin as studied by NMR spectroscopyIvano Bertini
CERM, University of Florence, Via Luigi Sacconi 6 50019 Sesto Fiorentino, Florence, Italy
Chemistry 9:2316-22. 2003....
Paramagnetic shifts in solid-state NMR of proteins to elicit structural informationStéphane Balayssac
Magnetic Resonance Center, University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Italy
Proc Natl Acad Sci U S A 105:17284-9. 2008..Furthermore, intermolecular pcs provide unique information on positions and orientations of neighboring protein molecules in the solid phase...
