4BH5

LytM domain of EnvC, an activator of cell wall amidases in Escherichia coli

4BH5 の概要

• エントリーDOI: 10.2210/pdb4bh5/pdb
• 分子名称: MUREIN HYDROLASE ACTIVATOR ENVC, IODIDE ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: cell cycle, amidase activator, autolysin, cytokinesis, morphogenesis, sacculus, peptidoglycan
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64292.85

構造登録者

Morlot, C.,Peters, N.T.,Yang, D.C.,Uehara, T.,Vernet, T.,Bernhardt, T.G. (登録日: 2013-03-29, 公開日: 2013-07-03, 最終更新日: 2023-12-20)

主引用文献

Peters, N.T.,Morlot, C.,Yang, D.C.,Uehara, T.,Vernet, T.,Bernhardt, T.G.
Structure-Function Analysis of the Lytm Domain of Envc, an Activator of Cell Wall Remodeling at the Escherichia Coli Division Site.
Mol.Microbiol., 89:690-, 2013

PubMed Abstract: Proteins with LytM (Peptidase_M23) domains are broadly distributed in bacteria and have been implicated in a variety of important processes, including cell division and cell-shape determination. Most LytM-like proteins that have been structurally and/or biochemically characterized are metallo-endopeptidases that cleave cross-links in the peptidoglycan (PG) cell wall matrix. Notable exceptions are the Escherichia coli cell division proteins EnvC and NlpD. These LytM factors are not hydrolases themselves, but instead serve as activators that stimulate PG cleavage by target enzymes called amidases to promote cell separation. Here we report the structure of the LytM domain from EnvC, the first structure of a LytM factor implicated in the regulation of PG hydrolysis. As expected, the fold is highly similar to that of other LytM proteins. However, consistent with its role as a regulator, the active-site region is degenerate and lacks a catalytic metal ion. Importantly, genetic analysis indicates that residues in and around this degenerate active site are critical for amidase activation in vivo and in vitro. Thus, in the regulatory LytM factors, the apparent substrate binding pocket conserved in active metallo-endopeptidases has been adapted to control PG hydrolysis by another set of enzymes.

PubMed: 23796240
DOI: 10.1111/MMI.12304

実験手法

X-RAY DIFFRACTION (1.57 Å)