Klemens Wild

Summary

Affiliation: University of Heidelberg
Country: Germany

Publications

  1. ncbi request reprint Crystal structure of an early protein-RNA assembly complex of the signal recognition particle
    K Wild
    Biochemie Zentrum BZH, University of Heidelberg, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
    Science 294:598-601. 2001
  2. doi request reprint Structural insights into the assembly of the human and archaeal signal recognition particles
    Klemens Wild
    Heidelberg University Biochemistry Center BZH, University of Heidelberg, INF328, D 69120 Heidelberg, Germany
    Acta Crystallogr D Biol Crystallogr 66:295-303. 2010
  3. ncbi request reprint A structural step into the SRP cycle
    Klemens Wild
    Biochemie Zentrum der Universität Heidelberg BZH, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
    Mol Microbiol 53:357-63. 2004
  4. doi request reprint The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis
    Gunes Bozkurt
    Heidelberg University Biochemistry Center BZH, Heidelberg, Germany
    FEBS Lett 584:1509-14. 2010
  5. pmc FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system
    Gert Bange
    Biochemie Zentrum der Universitat Heidelberg, INF328, 69120 Heidelberg, Germany
    Proc Natl Acad Sci U S A 107:11295-300. 2010
  6. ncbi request reprint The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains
    Oliver Schlenker
    Biochemie Zentrum der Universität Heidelberg BZH, Im Neuenheimer Feld 328, D 69120 Heidelberg, Germany
    J Biol Chem 281:8898-906. 2006
  7. pmc Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
    Ken R Rosendal
    Biochemie Zentrum Heidelberg, INF 328, D 69120 Heidelberg, Germany
    Proc Natl Acad Sci U S A 100:14701-6. 2003
  8. ncbi request reprint Crystal structure of the human Fe65-PTB1 domain
    Jens Radzimanowski
    Heidelberg University Biochemistry Center, INF328, D 69120 Heidelberg, Germany
    J Biol Chem 283:23113-20. 2008
  9. pmc Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation-associated protein Ebp1
    Eva Kowalinski
    Heidelberg University Biochemistry Center, INF 328, D 69120 Heidelberg, Germany
    Acta Crystallogr Sect F Struct Biol Cryst Commun 63:768-70. 2007
  10. pmc Overproduction, purification, crystallization and preliminary X-ray analysis of human Fe65-PTB2 in complex with the amyloid precursor protein intracellular domain
    Jens Radzimanowski
    Heidelberg University Biochemistry Center, INF328, D 69120 Heidelberg, Germany
    Acta Crystallogr Sect F Struct Biol Cryst Commun 64:409-12. 2008

Collaborators

Detail Information

Publications30

  1. ncbi request reprint Crystal structure of an early protein-RNA assembly complex of the signal recognition particle
    K 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...
  2. doi request reprint Structural insights into the assembly of the human and archaeal signal recognition particles
    Klemens 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...
  3. ncbi request reprint A structural step into the SRP cycle
    Klemens 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...
  4. doi request reprint The structure of Get4 reveals an alpha-solenoid fold adapted for multiple interactions in tail-anchored protein biogenesis
    Gunes 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...
  5. pmc FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system
    Gert 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...
  6. ncbi request reprint The structure of the mammalian signal recognition particle (SRP) receptor as prototype for the interaction of small GTPases with Longin domains
    Oliver Schlenker
    Biochemie Zentrum der Universität Heidelberg BZH, 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...
  7. pmc Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication
    Ken 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...
  8. ncbi request reprint Crystal structure of the human Fe65-PTB1 domain
    Jens 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...
  9. pmc Expression, purification, crystallization and preliminary crystallographic analysis of the proliferation-associated protein Ebp1
    Eva 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...
  10. pmc Overproduction, purification, crystallization and preliminary X-ray analysis of human Fe65-PTB2 in complex with the amyloid precursor protein intracellular domain
    Jens 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...
  11. pmc Purification, crystallization and preliminary structural characterization of the periplasmic domain P1 of the Escherichia coli membrane-protein insertase YidC
    Stephanie 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
    ....
  12. pmc Lipids trigger a conformational switch that regulates signal recognition particle (SRP)-mediated protein targeting
    Goran 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...
  13. ncbi request reprint SRP meets the ribosome
    Klemens Wild
    Biochemie Zentrum der Universitat Heidelberg, 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...
  14. ncbi request reprint The crystal structure of Ebp1 reveals a methionine aminopeptidase fold as binding platform for multiple interactions
    Eva 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...
  15. pmc Structure of the intracellular domain of the amyloid precursor protein in complex with Fe65-PTB2
    Jens 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...
  16. doi request reprint SRP RNA remodeling by SRP68 explains its role in protein translocation
    Jan Timo Grotwinkel
    Heidelberg University Biochemistry Center BZH, INF 328, D 69120 Heidelberg, Germany
    Science 344:101-4. 2014
    ..The ARM opens the conserved 5f RNA loop, which in ribosome-bound SRP establishes a contact to ribosomal RNA. Our data provide the structural basis for eukaryote-specific, SRP68-driven RNA remodeling required for protein translocation. ..
  17. pmc Structural insights into tail-anchored protein binding and membrane insertion by Get3
    Gunes 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...
  18. ncbi request reprint Crystallization of the crenarchaeal SRP core
    Ken 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...
  19. doi request reprint Structural basis for specific substrate recognition by the chloroplast signal recognition particle protein cpSRP43
    Katharina 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...
  20. pmc Membrane curvature induced by Arf1-GTP is essential for vesicle formation
    Rainer 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...
  21. pmc The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP
    Gert 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...
  22. doi request reprint Phosphorylation of LRP1 regulates the interaction with Fe65
    Wilfried Klug
    Heidelberg University Biochemistry Center BZH, Heidelberg, Germany
    FEBS Lett 585:3229-35. 2011
    ....
  23. ncbi request reprint Arx1 functions as an unorthodox nuclear export receptor for the 60S preribosomal subunit
    Bettina 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...
  24. ncbi request reprint Protein translocation: checkpoint role for SRP GTPase activation
    Gert 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...
  25. doi request reprint The crystal structure of the periplasmic domain of the Escherichia coli membrane protein insertase YidC contains a substrate binding cleft
    Stephanie 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...
  26. ncbi request reprint Towards the structure of the mammalian signal recognition particle
    Klemens Wild
    Biochemie Zentrum BZH, University of Heidelberg, Im Neuenheimer Feld 328, D 69120, Heidelberg, Germany
    Curr Opin Struct Biol 12:72-81. 2002
    ....
  27. pmc Mercury-induced crystallization and SAD phasing of the human Fe65-PTB1 domain
    Jens 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)...
  28. ncbi request reprint Following the signal sequence from ribosomal tunnel exit to signal recognition particle
    Mario 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...
  29. ncbi request reprint The structure of the chloroplast signal recognition particle (SRP) receptor reveals mechanistic details of SRP GTPase activation and a conserved membrane targeting site
    Katharina 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...
  30. pmc Expression, purification and preliminary crystallographic characterization of FlhF from Bacillus subtilis
    Gert 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...