2ZL4
Crystal structure of H.pylori ClpP S99A in complex with the peptide AAAA
Summary for 2ZL4
| Entry DOI | 10.2210/pdb2zl4/pdb |
| Related | 2ZL0 2ZL2 2ZL3 |
| Descriptor | ATP-dependent Clp protease proteolytic subunit, Peptide substrate AAAA (3 entities in total) |
| Functional Keywords | peptide substrate, tetra-ala, cytoplasm, hydrolase, protease, serine protease |
| Biological source | Helicobacter pylori More |
| Cellular location | Cytoplasm (By similarity): P56156 |
| Total number of polymer chains | 28 |
| Total formula weight | 305676.00 |
| Authors | |
| Primary citation | Kim, D.Y.,Kim, K.K. The structural basis for the activation and peptide recognition of bacterial ClpP J.Mol.Biol., 379:760-771, 2008 Cited by PubMed Abstract: 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. PubMed: 18468623DOI: 10.1016/j.jmb.2008.04.036 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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