1tzp
From Proteopedia
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MEPA, inactive form without ZN in P21
Overview
LAS enzymes are a group of metallopeptidases that share an active site, architecture and a core folding motif and have been named according to the, group members lysostaphin, D-Ala-D-Ala carboxypeptidase and sonic, hedgehog. Escherichia coli MepA is a periplasmic, penicillin-insensitive, murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl, amide bond in E. coli peptidoglycan. The enzyme lacks sequence similarity, with other peptidases, and is currently classified as a peptidase of, unknown fold and catalytic class in all major data bases. Here, we build, on our observation that two motifs, characteristic of the newly described, LAS group of metallopeptidases, are conserved in MepA-type sequences. We, demonstrate that recombinant E. coli MepA is sensitive to metal chelators, and that mutations in the predicted Zn2+ ligands His-113, Asp-120, and, His-211 inactivate the enzyme. Moreover, we present the crystal structure, of MepA. The active site of the enzyme is most similar to the active sites, of lysostaphin and D-Ala-D-Ala carboxypeptidase, and the fold is most, closely related to the N-domain of sonic hedgehog. We conclude that, MepA-type peptidases are LAS enzymes.
About this Structure
1TZP is a Single protein structure of sequence from Escherichia coli with SO4 and BU1 as ligands. Full crystallographic information is available from OCA.
Reference
Peptidoglycan amidase MepA is a LAS metallopeptidase., Marcyjaniak M, Odintsov SG, Sabala I, Bochtler M, J Biol Chem. 2004 Oct 15;279(42):43982-9. Epub 2004 Jul 29. PMID:15292190
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