2zl2: Difference between revisions
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'''Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ''' | '''Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ''' | ||
==Overview== | |||
ClpP and its ATPase compartment, ClpX or ClpA, remove misfolded proteins in cells and are of utmost importance in protein quality control. The ring hexamers of ClpA or ClpX recognize, unfold, and translocate target substrates into the degradation chamber of the double-ring tetradecamer of ClpP. The overall reaction scheme catalyzed by ClpXP or ClpAP has been proposed; however, the molecular mechanisms associated with substrate recognition and degradation have not yet been clarified in detail. To investigate these mechanisms, we determined the crystal structures of ClpP from Helicobacter pylori in complex with product peptides bound to the active site as well as in the apo state. In the complex structure, the peptides are zipped with two antiparallel strands of ClpP and point to the adjacent active site, thus providing structural explanations for the broad substrate specificity, the product inhibition and the processive degradation of substrates in the chamber. The structures also suggest that substrate binding causes local conformational changes around the active site that ultimately induce the active conformation of ClpP. | |||
==About this Structure== | ==About this Structure== | ||
2ZL2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL2 OCA]. | 2ZL2 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZL2 OCA]. | ||
==Reference== | |||
The structural basis for the activation and peptide recognition of bacterial ClpP., Kim DY, Kim KK, J Mol Biol. 2008 Jun 13;379(4):760-71. Epub 2008 Apr 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18468623 18468623] | |||
[[Category: Endopeptidase Clp]] | [[Category: Endopeptidase Clp]] | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
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[[Category: Protease]] | [[Category: Protease]] | ||
[[Category: Serine protease]] | [[Category: Serine protease]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 18 12:19:41 2008'' | ||
Revision as of 12:19, 18 June 2008
Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ
OverviewOverview
ClpP and its ATPase compartment, ClpX or ClpA, remove misfolded proteins in cells and are of utmost importance in protein quality control. The ring hexamers of ClpA or ClpX recognize, unfold, and translocate target substrates into the degradation chamber of the double-ring tetradecamer of ClpP. The overall reaction scheme catalyzed by ClpXP or ClpAP has been proposed; however, the molecular mechanisms associated with substrate recognition and degradation have not yet been clarified in detail. To investigate these mechanisms, we determined the crystal structures of ClpP from Helicobacter pylori in complex with product peptides bound to the active site as well as in the apo state. In the complex structure, the peptides are zipped with two antiparallel strands of ClpP and point to the adjacent active site, thus providing structural explanations for the broad substrate specificity, the product inhibition and the processive degradation of substrates in the chamber. The structures also suggest that substrate binding causes local conformational changes around the active site that ultimately induce the active conformation of ClpP.
About this StructureAbout this Structure
2ZL2 is a Protein complex structure of sequences from Helicobacter pylori. Full crystallographic information is available from OCA.
ReferenceReference
The structural basis for the activation and peptide recognition of bacterial ClpP., Kim DY, Kim KK, J Mol Biol. 2008 Jun 13;379(4):760-71. Epub 2008 Apr 20. PMID:18468623 Page seeded by OCA on Wed Jun 18 12:19:41 2008