5OQ1
Crystal structure of Serratia marcescens ChiX (used as MR model for superior PDB 5OPZ)
5OQ1 の概要
エントリーDOI | 10.2210/pdb5oq1/pdb |
関連するPDBエントリー | 5OPZ |
分子名称 | ChiX, ZINC ION, CHLORIDE ION, ... (4 entities in total) |
機能のキーワード | l-ala d-glu endopeptidase serratia marcescens chitinase secretion anomalous dispersion zinc enzyme, hydrolase |
由来する生物種 | Serratia marcescens |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 31135.57 |
構造登録者 | Owen, R.A.,Fyfe, P.K.,Lodge, A.,Biboy, J.,Vollmer, W.,Hunter, W.N.,Sargent, F. (登録日: 2017-08-10, 公開日: 2018-01-17, 最終更新日: 2024-05-08) |
主引用文献 | Owen, R.A.,Fyfe, P.K.,Lodge, A.,Biboy, J.,Vollmer, W.,Hunter, W.N.,Sargent, F. Structure and activity of ChiX: a peptidoglycan hydrolase required for chitinase secretion by Serratia marcescens. Biochem. J., 475:415-428, 2018 Cited by PubMed Abstract: The Gram-negative bacterium secretes many proteins that are involved in extracellular chitin degradation. This so-called chitinolytic machinery includes three types of chitinase enzymes and a lytic polysaccharide monooxygenase. An operon has been identified in , , that is thought to be involved in the secretion of the chitinolytic machinery. Genetic evidence points to the ChiX protein being a key player in the secretion mechanism, since deletion of the gene in led to a mutant strain blocked for secretion of all members of the chitinolytic machinery. In this work, a detailed structural and biochemical characterisation of ChiX is presented. The high-resolution crystal structure of ChiX reveals the protein to be a member of the LAS family of peptidases. ChiX is shown to be a zinc-containing metalloenzyme, and assays demonstrate that ChiX is an l-Ala d-Glu endopeptidase that cleaves the cross-links in bacterial peptidoglycan. This catalytic activity is shown to be intimately linked with the secretion of the chitinolytic machinery, since substitution of the ChiX Asp-120 residue results in a variant protein that is both unable to digest peptidoglycan and cannot rescue the phenoytype of a mutant strain. PubMed: 29229757DOI: 10.1042/BCJ20170633 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.34 Å) |
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