2ZL2

Crystal structure of H.pylori ClpP in complex with the peptide NVLGFTQ

2ZL2 の概要

• エントリーDOI: 10.2210/pdb2zl2/pdb
• 関連するPDBエントリー: 2ZL0 2ZL2 2ZL3
• 分子名称: ATP-dependent Clp protease proteolytic subunit, A peptide substrate-NVLGFTQ, A peptide substrate-NVLGFTQ for Chain R and S (3 entities in total)
• 機能のキーワード: peptide substrate, cytoplasm, hydrolase, protease, serine protease
• 由来する生物種: Helicobacter pylori; 詳細
• 細胞内の位置: Cytoplasm (By similarity): P56156
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 309117.85

構造登録者

Kim, D.Y.,Kim, K.K. (登録日: 2008-04-02, 公開日: 2008-04-22, 最終更新日: 2023-11-01)

主引用文献

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

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: 18468623
DOI: 10.1016/j.jmb.2008.04.036

実験手法

X-RAY DIFFRACTION (2.5 Å)