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Publication Abstract from PubMed

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.

Structure and mechanism of the caseinolytic protease ClpP1/2 heterocomplex from Listeria monocytogenes.,Dahmen M, Vielberg MT, Groll M, Sieber SA Angew Chem Int Ed Engl. 2015 Mar 16;54(12):3598-602. doi: 10.1002/anie.201409325., Epub 2015 Jan 28. PMID:25630955^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.