4RYF

ClpP1/2 heterocomplex from Listeria monocytogenes

Summary for 4RYF

• Entry DOI: 10.2210/pdb4ryf/pdb
• Related: 2FZS 4JCQ 4JCT
• Descriptor: ATP-dependent Clp protease proteolytic subunit, SODIUM ION, MALONATE ION, ... (5 entities in total)
• Functional Keywords: pathogenic bacteria, enzyme catalysis, proteolysis, ser-protease, heterocomplex, clpp, hydrolase
• Biological source: Listeria monocytogenes; More
• Total number of polymer chains: 14
• Total formula weight: 317228.18

Authors

Dahmen, M.,Vielberg, M.-T.,Groll, M.,Sieber, S.A. (deposition date: 2014-12-15, release date: 2014-12-31, Last modification date: 2023-09-20)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)