1U10

MEPA, active form with ZN in P1

1U10 の概要

• エントリーDOI: 10.2210/pdb1u10/pdb
• 関連するPDBエントリー: 1TZP
• 分子名称: Penicillin-insensitive murein endopeptidase, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: las enzyme, metallopeptidase, peptidoglycan hydrolase, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P14007
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 172841.94

構造登録者

Marcyjaniak, M.,Odintsov, S.G.,Sabala, I.,Bochtler, M. (登録日: 2004-07-14, 公開日: 2004-09-07, 最終更新日: 2024-10-30)

主引用文献

Marcyjaniak, M.,Odintsov, S.G.,Sabala, I.,Bochtler, M.
Peptidoglycan amidase MepA is a LAS metallopeptidase
J.Biol.Chem., 279:43982-43989, 2004

PubMed Abstract: 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.

PubMed: 15292190
DOI: 10.1074/jbc.M406735200

実験手法

X-RAY DIFFRACTION (2.4 Å)