4RYF

ClpP1/2 heterocomplex from Listeria monocytogenes

4RYF の概要

• エントリーDOI: 10.2210/pdb4ryf/pdb
• 関連するPDBエントリー: 2FZS 4JCQ 4JCT
• 分子名称: ATP-dependent Clp protease proteolytic subunit, SODIUM ION, MALONATE ION, ... (5 entities in total)
• 機能のキーワード: pathogenic bacteria, enzyme catalysis, proteolysis, ser-protease, heterocomplex, clpp, hydrolase
• 由来する生物種: Listeria monocytogenes; 詳細
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 317228.18

構造登録者

Dahmen, M.,Vielberg, M.-T.,Groll, M.,Sieber, S.A. (登録日: 2014-12-15, 公開日: 2014-12-31, 最終更新日: 2023-09-20)

主引用文献

Dahmen, M.,Vielberg, M.T.,Groll, M.,Sieber, S.A.
Structure and mechanism of the caseinolytic protease ClpP1/2 heterocomplex from Listeria monocytogenes.
Angew.Chem.Int.Ed.Engl., 54:3598-3602, 2015

PubMed Abstract: Listeria monocytogenes is a devastating bacterial pathogen. Its virulence and intracellular stress tolerance are supported by caseinolytic protease P (ClpP), an enzyme that is conserved among bacteria. L. monocytogenes expresses two ClpP isoforms that are only distantly related by sequence and differ in catalysis, oligomerization, active-site composition, and N-terminal interaction sites for associated AAA(+) chaperones. The crystal structure of the ClpP1/2 heterocomplex from L. monocytogenes was solved, and in combination with biochemical studies, it provides insights into the mode of action. The results demonstrate that structural interlocking of LmClpP1 with LmClpP2 leads to the formation of a tetradecamer, aligns all 14 active sites, and enhances proteolytic activity. Furthermore, the catalytic center was identified as being responsible for the transient stability of ClpPs.

PubMed: 25630955
DOI: 10.1002/anie.201409325

実験手法

X-RAY DIFFRACTION (2.8 Å)