Research Topics
Genomes and GenesSpecies | S Samar HasnainSummaryAffiliation: CCLRC Daresbury Laboratory Country: UK Publications
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Detail Information
Publications
XAFS studies of nitrogenase: the MoFe and VFe proteins and the use of crystallographic coordinates in three-dimensional EXAFS data analysisRichard W Strange
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK
J Synchrotron Radiat 10:71-5. 2003..Thus, the VFe protein of V-nitrogenase has been shown by EXAFS to possess a V-atom site catalytically similar to the well characterized MoFe-nitrogenases, with V replacing Mo...- Synchrotron techniques for metalloproteins and human disease in post genome eraS Samar Hasnain
Molecular Biophysics Group and North West Structural Genomics Centre, CCLRC Daresbury Laboratory, Warrington WA4 4AD, UK
J Synchrotron Radiat 11:7-11. 2004..In this context, the benefits of adopting the 'philosophy' being developed for the structural genomics effort are highlighted... - Marriage of XAFS and crystallography for structure-function studies of metalloproteinsS Samar Hasnain
College of Biology and Medicine, CLRC Daresbury Laboratory, Warrington WA4 4AD, UK
J Synchrotron Radiat 10:9-15. 2003.... - Variable metallation of human superoxide dismutase: atomic resolution crystal structures of Cu-Zn, Zn-Zn and as-isolated wild-type enzymesRichard W Strange
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK
J Mol Biol 356:1152-62. 2006..These data raise the possibility that in a cellular environment with low availability of free copper, Zn-Zn may be the preferred metallation state of SOD1 prior to its interaction with the copper chaperone... 
Structural consequences of the familial amyotrophic lateral sclerosis SOD1 mutant His46ArgSvetlana Antonyuk
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire, WA4 4AD, UK
Protein Sci 14:1201-13. 2005....- Combined use of XAFS and crystallography for studying protein-ligand interactions in metalloproteinsRichard W Strange
Molecular Biophysics Group, College of Biology and Medicine, CCLRC Daresbury Laboratory, Daresbury, Warrington, Cheshire, UK
Methods Mol Biol 305:167-96. 2005.... 
On-line optical and X-ray spectroscopies with crystallography: an integrated approach for determining metalloprotein structures in functionally well defined statesMark J Ellis
Molecular Biophysics Group, STFC Daresbury Laboratory, Warrington WA4 4AD, UK
J Synchrotron Radiat 15:433-9. 2008..This example clearly demonstrates the importance of using two on-line methods, spectroscopy and XAS, for identifying well defined redox states of metalloproteins during crystallographic data collection...- Observation of an unprecedented Cu Bis-His site: crystal structure of the H129V mutant of nitrite reductaseMark J Ellis
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire, UK
Inorg Chem 43:7591-3. 2004..We have mutated one of the type 2 copper ligating histidines to observe the effect on catalytic turnover. This mutation has created a unique site where Cu is ligated by 2 His Nepsilon2 atoms alone... - The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosisRichard W Strange
Molecular Biophysics Group, Department of Synchrotron Radiation, CCLRC Daresbury Laboratory, Warrington, Cheshire, UK
J Mol Biol 328:877-91. 2003.... - A high-throughput structural biology/proteomics beamline at the SRS on a new multipole wigglerMichele Cianci
CCLRC Daresbury Laboratory, Warrington WA4 4AD, Cheshire, UK
J Synchrotron Radiat 12:455-66. 2005..0-2.5 A softer wavelength range. This range also covers the K-edges of a number of important 3d transition metals as well as the L-edges of xenon and iodine and enhanced sulfur f ''... - Electron donation between copper containing nitrite reductases and cupredoxins: the nature of protein-protein interaction in complex formationLoretta M Murphy
CLRC Daresbury Laboratory, Warrington, Cheshire, UK
J Mol Biol 315:859-71. 2002..These results are discussed in terms of surface compatibility of the component proteins, complex formation, overall charges, charge distribution, hydrophobic patches and redox potentials. A docking model for the complexes is proposed... - The N-terminal extension of rusticyanin is not responsible for its acid stabilityJ Gunter Grossmann
Synchrotron Radiation Department, CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK
Biochemistry 41:3613-9. 2002..The mutant does not bind copper. These results provide evidence that the unique N-terminus of rusticyanin is not responsible for the acid stability of the hydrophobic beta-barrel core of the protein... - Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALSJennifer Stine Elam
Department of Biochemistry and the Center for Biomolecular Structure Analysis, The University of Texas, Health Science Center at San Antonio, 7703 Floyd Curl Drive, San Antonio, Texas 78229 3900, USA
Nat Struct Biol 10:461-7. 2003..Loss of this protection through conformational rearrangement in the metal-deficient enzyme could be a toxic property common to mutants of SOD1 linked to FALS... - Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosisXiaohang Cao
Department of Biochemistry and the X ray Crystallography Core Laboratory, The University of Texas Health Ssience Center, San Antonio, Texas 78229, USA
J Biol Chem 283:16169-77. 2008..These findings support the notion that metal-deficient and/or disulfide-reduced mutant SOD1 species contribute to toxicity in SOD1-linked amyotrophic lateral sclerosis... - Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutaseRichard W Strange
Molecular Biophysics Group and Department of Computational Science and Engineering, Science and Technology Facilities Council, Daresbury Laboratory, Warrington, Cheshire WA4 4AD, United Kingdom
Proc Natl Acad Sci U S A 104:10040-4. 2007..This result also has implications for the role of demetallated wild-type SOD1 in sporadic cases of ALS, for which the molecular cause still remains undiscovered... - Insight into catalysis of nitrous oxide reductase from high-resolution structures of resting and inhibitor-bound enzyme from Achromobacter cycloclastesKonstantinos Paraskevopoulos
School of Biomolecular Sciences, Liverpool John Moores University, Liverpool L3 5AF, UK
J Mol Biol 362:55-65. 2006..These structures, together with the published structural and spectroscopic data, give fresh insight into the mode of substrate binding, reduction and catalysis... - Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual propertiesMark L Barrett
School of Health and Life Sciences, De Montfort University, The Gateway, Leicester, UK
Biochemistry 45:2927-39. 2006..The structural and energetic effects of mutating the equatorial cysteine to serine, yet to be studied experimentally, are predicted to be considerable by our calculations... - Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanismMark J Ellis
Faculty of Applied Science, De Montfort University, Leicester, LE1 9BH, UK
J Mol Biol 316:51-64. 2002..The H254F and D92N mutant structures provide, for the first time, observation of surface Zn sites which may act as a Zn sink and prevent binding of Zn at the catalytic Cu site in the native enzyme... - Insights into redox partner interactions and substrate binding in nitrite reductase from Alcaligenes xylosoxidans: crystal structures of the Trp138His and His313Gln mutantsMark L Barrett
Faculty of Applied Sciences, De Montfort University, The Gateway, Leicester, LE1 9BH, United Kingdom
Biochemistry 43:16311-9. 2004..65 and 1.72 A, respectively. The observation of the substrate-bound structure for the His313Gln mutant and inhibitory studies with PEG establishes the role of the hydrophobic pocket as the port of substrate entry... - Crystal structures of the Met148Leu and Ser86Asp mutants of rusticyanin from Thiobacillus ferrooxidans: insights into the structural relationship with the cupredoxins and the multi copper proteinsLalji D Kanbi
Faculty of Applied Sciences, De Montfort University, The Gateway, Leicester LE1 9BH, UK
J Mol Biol 320:263-75. 2002..We confirm that rusticyanin is in the same class as nitrite reductase domain 2, laccase domain 3 and ceruloplasmin domains 2, 4 and 6... - Heterologous metalloprotein biosynthesis in Escherichia coli: conditions for the overproduction of functional copper-containing nitrite reductase and azurin from Alcaligenes xylosoxidansRoger L Harris
Department of Molecular Microbiology, John Innes Centre, Norwich NR4 7UH, UK
J Synchrotron Radiat 12:13-8. 2005..xylosoxidans. The findings of this work have important implications for the overproduction of recombinant metalloproteins in heterologous hosts... - Towards the high-throughput expression of metalloproteins from the Mycobacterium tuberculosis genomeJohn F Hall
Cell Signalling Laboratory, De Montfort University, Leicester LE1 9BH, UK
J Synchrotron Radiat 12:4-7. 2005..Alternative purification systems are also required and the properties of a mutant blue copper protein are described, that may offer a combined purification and tagging system... - Dimer destabilization in superoxide dismutase may result in disease-causing properties: structures of motor neuron disease mutantsMichael A Hough
Molecular Biophysics Group, Council for the Central Laboratory of the Research Councils, Daresbury Laboratory, Warrington, Cheshire WA4 4AD, United Kingdom
Proc Natl Acad Sci U S A 101:5976-81. 2004.... - Structure of fully reduced bovine copper zinc superoxide dismutase at 1.15 AMichael A Hough
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Daresbury, Warrington, Cheshire, WA4 4AD, United Kingdom
Structure 11:937-46. 2003..65 A) has allowed a more detailed examination of the metal center environment and its associated water network in the active site channel, facilitating the analysis of potential proton transfer routes... - The structure of glyceraldehyde 3-phosphate dehydrogenase from Alcaligenes xylosoxidans at 1.7 A resolutionSvetlana V Antonyuk
Molecular Biophysics Group, CCLRC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, England
Acta Crystallogr D Biol Crystallogr 59:835-42. 2003..stearothermophilus. One half-occupancy sulfate ion is also located in the substrate-binding site of monomer P... - Crystallography with online optical and X-ray absorption spectroscopies demonstrates an ordered mechanism in copper nitrite reductaseMichael A Hough
Molecular Biophysics Group, STFC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK
J Mol Biol 378:353-61. 2008.... - Modulation of NO binding to cytochrome c' by distal and proximal haem pocket residuesSonia Barbieri
Molecular Biophysics Group, STFC Daresbury Laboratory, Warrington, Cheshire WA4 4AD, UK
J Biol Inorg Chem 13:531-40. 2008..In contrast, the R124L substitution retained the property of the native protein in the initial formation of a six-coordinate NO adduct, a finding of functional importance since a Lys or an Arg residue is invariant in these proteins... - Genomic analysis reveals widespread occurrence of new classes of copper nitrite reductasesMark J Ellis
Molecular Biophysics Group, Science and Technology Facilities Council, Daresbury Laboratory, Warrington, Cheshire, UK
J Biol Inorg Chem 12:1119-27. 2007.... - The structure of the Met144Leu mutant of copper nitrite reductase from Alcaligenes xylosoxidans provides the first glimpse of a protein-protein complex with azurin IIKonstantinos Paraskevopoulos
Molecular Biophysics Group, STFC Daresbury Laboratory, Warrington, UK
J Biol Inorg Chem 12:789-96. 2007.... - X-ray structure analysis of a metalloprotein with enhanced active-site resolution using in situ x-ray absorption near edge structure spectroscopyAlessandro Arcovito
Department of Biochemical Sciences and Consiglio Nazionale delle Ricerche, Institute of Molecular Biology and Pathology, University of Rome La Sapienza, P le A Moro 5, 00185 Rome, Italy
Proc Natl Acad Sci U S A 104:6211-6. 2007.... - Atomic resolution structures of native copper nitrite reductase from Alcaligenes xylosoxidans and the active site mutant Asp92GluMark J Ellis
Faculty of Applied Science, De Montfort University, Leicester LE1 9BH, UK
J Mol Biol 328:429-38. 2003..04, 1.15 and 1.12A resolutions, respectively. These structures provide the basis from which to build a detailed mechanism of this important enzyme... - Introductory overview: X-ray absorption spectroscopy and structural genomicsIsabella Ascone
LURE, Bâtiment 209E, Universite Paris Sud, 91898 Orsay Cedex, France
J Synchrotron Radiat 10:1-3. 2003..The Issue confirms that BioXAS has come of age and it can be expected to make a significant contribution in the structural genomics effort on metalloproteins, which are estimated to make up about 30% of proteins coded by genomes... - Metal-ligand interplay in blue copper proteins studied by 1H NMR spectroscopy: Cu(II)-pseudoazurin and Cu(II)-rusticyaninAntonio Donaire
, University of Rosario, Suipacha 531, S2002LRK Rosario, Argentina
J Am Chem Soc 124:13698-708. 2002..Finally, the observed chemical shifts for beta-CH(2) Cys and Ser NH protons in rusticyanin suggest that a less negative charge at the sulfur atom could contribute to the high redox potential (680 mV) of this protein... - Resolution improvement from 'in situ annealing' of copper nitrite reductase crystalsMark J Ellis
Faculty of Applied Science, De Montfort University, Leicester LE1 9BH, England
Acta Crystallogr D Biol Crystallogr 58:456-8. 2002..The effective resolution limits increased by 1.5 A from 2.5 to 1.0 A, the mosaicity value decreased from 1.5 to 0.3 degree and the spot shape changed from elliptical to circular...