Research Topics
Genomes and Genes | Klemens WildSummaryAffiliation: University of Heidelberg Country: Germany Publications
| Collaborators
|
Detail Information
Publications
Crystal structure of an early protein-RNA assembly complex of the signal recognition particleK Wild
Biochemie Zentrum BZH, University of Heidelberg, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
Science 294:598-601. 2001..A model of the assembly of the SRP core comprising SRP19, SRP54, and SRP RNA based on crystallographic and biochemical data is proposed...
Structural insights into the assembly of the human and archaeal signal recognition particlesKlemens Wild
Heidelberg University Biochemistry Center BZH, University of Heidelberg, INF328, D 69120 Heidelberg, Germany
Acta Crystallogr D Biol Crystallogr 66:295-303. 2010..Differences in SRP assembly between mammalia and archaea are therefore independent of SRP19 and are based on differences in SRP RNA itself. A new SRP-assembly scheme is presented...- A structural step into the SRP cycleKlemens Wild
Biochemie Zentrum der Universität Heidelberg BZH, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
Mol Microbiol 53:357-63. 2004..The model is placed in the context of the recent structures of mammalian SRP bound to a ribosome-nascent chain complex and of a subcomplex of SRP-SR... - The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesisGunes Bozkurt
Heidelberg University Biochemistry Center BZH, Heidelberg, Germany
FEBS Lett 584:1509-14. 2010..A conserved hydrophobic groove accommodates the flexible C-terminal region in trans. The structural organization of the Get4 helical hairpin motifs provides a scaffold for protein-protein interactions in the Get pathway... 
Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation-associated protein Ebp1Eva Kowalinski
Heidelberg University Biochemistry Center, INF 328, D 69120 Heidelberg, Germany
Acta Crystallogr Sect F Struct Biol Cryst Commun 63:768-70. 2007..Initially observed crystals were improved by serial seeding to single crystals suitable for data collection. The optimized crystals belong to the tetragonal space group P4(1)2(1)2 or P4(3)2(1)2 and diffracted to a resolution of 1.6 A...- Crystal structure of the human Fe65-PTB1 domainJens Radzimanowski
Heidelberg University Biochemistry Center, INF328, D 69120 Heidelberg, Germany
J Biol Chem 283:23113-20. 2008..We suggest Fe65-PTB1 to interact with its target proteins involved in translocation and signaling of APP in a phosphorylation-dependent manner... - FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion systemGert Bange
Biochemie Zentrum der Universitat Heidelberg, INF328, 69120 Heidelberg, Germany
Proc Natl Acad Sci U S A 107:11295-300. 2010..Taken together, these results allow to propose a model that explains how the T3SS may switch from the stoichiometric export of FliD to the high-throughput secretion of flagellin... - The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domainsOliver Schlenker
, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
J Biol Chem 281:8898-906. 2006..Based on structural conservation we present the SRbeta-GTP:SRX structure as a prototype for conserved interactions in a variety of GTPase regulated targeting events occurring at endomembranes... - Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communicationKen R Rosendal
Biochemie Zentrum Heidelberg, INF 328, D 69120 Heidelberg, Germany
Proc Natl Acad Sci U S A 100:14701-6. 2003..Hinge regions are identified in the linker between the G and M domains (292-LGMGD) and in the N-terminal part of the M domain, which allow for structural rearrangements within SRP54 upon signal peptide binding at the ribosome... - SRP meets the ribosomeKlemens Wild
, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
Nat Struct Mol Biol 11:1049-53. 2004..By combining structures of free and ribosome-bound SRP we derive a structural model describing the dynamic nature of SRP when it meets the ribosome... - Overproduction, purification, crystallization and preliminary X-ray analysis of human Fe65-PTB2 in complex with the amyloid precursor protein intracellular domainJens Radzimanowski
Heidelberg University Biochemistry Center, INF328, D 69120 Heidelberg, Germany
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:409-12. 2008..1 A resolution. Initial phases obtained by the molecular-replacement method are of good quality and revealed well defined electron density for the substrate peptide... - Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidCStephanie Ravaud
Biochemie Zentrum der Universität Heidelberg BZH, INF 328, D 69120 Heidelberg, Germany
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:144-8. 2008.... - Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targetingGoran Stjepanovic
Biochemie Zentrum BZH, University of Heidelberg, INF 328, 69120 Heidelberg, Germany
J Biol Chem 286:23489-97. 2011..Our results underline the dynamics of lipid-protein interactions and their importance in the regulation of protein targeting and translocation across biological membranes... - Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2Jens Radzimanowski
Heidelberg University Biochemistry Center, University of Heidelberg, INF328, D 69120 Heidelberg, Germany
EMBO Rep 9:1134-40. 2008..A molecular switch model is proposed... - The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactionsEva Kowalinski
Heidelberg University Biochemistry Center BZH, INF 328, D 69120 Heidelberg, Germany
FEBS Lett 581:4450-4. 2007..The structure provides insights in how Ebp1 discriminates between its different interaction partners... - Membrane curvature induced by Arf1-GTP is essential for vesicle formationRainer Beck
Biochemistry Center, Heidelberg University, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
Proc Natl Acad Sci U S A 105:11731-6. 2008..Strikingly, this mutant was not able to deform membranes, suggesting that GTP-induced dimerization of Arf1 is a critical step inducing membrane curvature during the formation of coated vesicles... - Crystallization of the crenarchaeal SRP coreKen R Rosendal
Biochemie-Zentrum (BZH, University of Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany
Acta Crystallogr D Biol Crystallogr 60:140-3. 2004..The tetartohedral twinning is enabled by a special diamond-like packing in a trigonal crystal... - Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43Katharina F Stengel
Biochemie Zentrum der Universitat Heidelberg, INF328, D 69120 Heidelberg, Germany
Science 321:253-6. 2008..We describe how cpSPR43 adapts the universally conserved SRP system to posttranslational targeting and insertion of the LHCP family of membrane proteins... - The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTPGert Bange
Heidelberg University Biochemistry Center BZH, INF 328, 69120 Heidelberg, Germany
Proc Natl Acad Sci U S A 104:13621-5. 2007..Our results provide insights into SRP GTPases and their roles in two fundamentally different protein-targeting routes that both rely on efficient protein delivery to a secretion channel... - Structural insights into tail-anchored protein binding and membrane insertion by Get3Gunes Bozkurt
Heidelberg University Biochemistry Center, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
Proc Natl Acad Sci U S A 106:21131-6. 2009..We postulate that ATP hydrolysis is needed to release Get3 from its receptor. Taken together, our results provide mechanistic insights into posttranslational targeting of TA membrane proteins by Get3... - Phosphorylation of LRP1 regulates the interaction with Fe65Wilfried Klug
Heidelberg University Biochemistry Center BZH, Heidelberg, Germany
FEBS Lett 585:3229-35. 2011.... - Arx1 functions as an unorthodox nuclear export receptor for the 60S preribosomal subunitBettina Bradatsch
Biochemie Zentrum der Universitat Heidelberg, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
Mol Cell 27:767-79. 2007..In contrast, the predicted central cavity of Arx1 is involved in the interaction with FG repeat nucleoporins and 60S subunit export. Thus, an ancient enzyme fold has been adopted by Arx1 to function as a nuclear export receptor... - The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleftStephanie Ravaud
Biochemie Zentrum der Universitat Heidelberg, Im Neuenheimer Feld 328, Heidelberg, Germany
J Biol Chem 283:9350-8. 2008..The analysis of this region suggests a role in membrane interaction and/or in the regulation of YidC interaction with binding partners... - Protein translocation: checkpoint role for SRP GTPase activationGert Bange
Heidelberg University Biochemistry Center BZH, INF328, D 69120 Heidelberg, Germany
Curr Biol 17:R980-2. 2007..A recent study provides new insights on the link between the GTPases and protein translocation... - Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domainJens Radzimanowski
Heidelberg University Biochemistry Center, INF328, D 69120 Heidelberg, Germany
Acta Crystallogr Sect F Struct Biol Cryst Commun 64:382-5. 2008..2 A resolution. SAD phases have been computed to the diffraction limit at the wavelength of maximum absorption (L(III) edge)... - Towards the structure of the mammalian signal recognition particleKlemens Wild
Biochemie-Zentrum (BZH, University of Heidelberg, Im Neuenheimer Feld 328, D-69120, Heidelberg, Germany
Curr Opin Struct Biol 12:72-81. 2002.... - The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting siteKatharina F Stengel
Biochemie Zentrum der Universitat Heidelberg, INF 328, D 69120, Heidelberg, Germany
FEBS Lett 581:5671-6. 2007..In cpFtsY this motif is extended, which might be responsible for the enhanced attachment of the protein to the thylakoid membrane... - Following the signal sequence from ribosomal tunnel exit to signal recognition particleMario Halic
Gene Center, Department of Chemistry and Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany
Nature 444:507-11. 2006..These findings provide the structural basis for improving our understanding of the early steps of co-translational protein sorting... - Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilisGert Bange
Heidelberg University Biochemistry Centre BZH, INF 328, 69120 Heidelberg, Germany
Acta Crystallogr Sect F Struct Biol Cryst Commun 63:449-51. 2007..Three crystal forms are reported with either GDP or GMPPNP and diffract to a resolution of about 3 A...