4jcr | pdb_00004jcr

ClpP1 N165D mutant from Listeria monocytogenes

spinqualitylabelsall models 4jcr, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4jcr is a 14 chain structure with sequence from Listeria monocytogenes egd-e. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 3v5e, 2fzs, 1tyf, 4jcq Gene: clpP, lmo1138 (Listeria monocytogenes EGD-e) Activity: Endopeptidase Clp, with EC number 3.4.21.92 Resources: FirstGlance, OCA, RCSB, PDBsum Function [Q8Y7Y1_LISMO] Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).[HAMAP-Rule:MF_00444] Publication Abstract from PubMed Caseinolytic proteases (ClpPs) are large oligomeric protein complexes that contribute to cell homeostasis as well as virulence regulation in bacteria. Although most organisms possess a single ClpP protein, some organisms encode two or more ClpP isoforms. Here, we elucidated the crystal structures of ClpP1 and ClpP2 from pathogenic Listeria monocytogenes and observe an unprecedented regulation principle by the catalytic triad. Whereas L. monocytogenes (Lm)ClpP2 is both structurally and functionally similar to previously studied tetradecameric ClpP proteins from Escherichia coli and Staphylococcus aureus, heptameric LmClpP1 features an asparagine in its catalytic triad. Mutation of this asparagine to aspartate increased the reactivity of the active site and led to the assembly of a tetradecameric complex. We analyzed the heterooligomeric complex of LmClpP1 and LmClpP2 via coexpression and subsequent labeling studies with natural product-derived probes. Notably, the LmClpP1 peptidase activity is stimulated 75-fold in the complex providing insights into heterooligomerization as a regulatory mechanism. Collectively, our data point toward different preferences for substrates and inhibitors of the two ClpP enzymes and highlight their structural and functional characteristics. Structural and functional insights into caseinolytic proteases reveal an unprecedented regulation principle of their catalytic triad.,Zeiler E, List A, Alte F, Gersch M, Wachtel R, Poreba M, Drag M, Groll M, Sieber SA Proc Natl Acad Sci U S A. 2013 Jul 9;110(28):11302-7. doi:, 10.1073/pnas.1219125110. Epub 2013 Jun 24. PMID:23798410 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Clp Protease

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