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5AA4

Crystal structure of MltF from Pseudomonas aeruginosa in complex with cell-wall tetrapeptide

5AA4 の概要
エントリーDOI10.2210/pdb5aa4/pdb
関連するPDBエントリー5AA1 5AA2 5AA3
分子名称MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F, [6-[[(2~{R})-1-azanyl-1-oxidanylidene-propan-2-yl]amino]-6-oxidanylidene-5-[[(4~{R})-5-oxidanyl-5-oxidanylidene-4-[[(2~{S})-2-[[(2~{R})-2-oxidanylpropanoyl]amino]propanoyl]amino]pentanoyl]amino]hexyl]azanium, ... (4 entities in total)
機能のキーワードlyase, lytic transglycosilase, cell wall recycling
由来する生物種PSEUDOMONAS AERUGINOSA
詳細
タンパク質・核酸の鎖数4
化学式量合計205003.17
構造登録者
Dominguez-Gil, T.,Acebron, I.,Hermoso, J.A. (登録日: 2015-07-23, 公開日: 2016-10-12, 最終更新日: 2024-01-10)
主引用文献Dominguez-Gil, T.,Lee, M.,Acebron-Avalos, I.,Mahasenan, K.V.,Hesek, D.,Dik, D.A.,Byun, B.,Lastochkin, E.,Fisher, J.F.,Mobashery, S.,Hermoso, J.A.
Activation by Allostery in Cell-Wall Remodeling by a Modular Membrane-Bound Lytic Transglycosylase from Pseudomonas aeruginosa.
Structure, 24:1729-1741, 2016
Cited by
PubMed Abstract: Bacteria grow and divide without loss of cellular integrity. This accomplishment is notable, as a key component of their cell envelope is a surrounding glycopeptide polymer. In Gram-negative bacteria this polymer-the peptidoglycan-grows by the difference between concurrent synthesis and degradation. The regulation of the enzymatic ensemble for these activities is poorly understood. We report herein the structural basis for the control of one such enzyme, the lytic transglycosylase MltF of Pseudomonas aeruginosa. Its structure comprises two modules: an ABC-transporter-like regulatory module and a catalytic module. Occupancy of the regulatory module by peptidoglycan-derived muropeptides effects a dramatic and long-distance (40 Å) conformational change, occurring over the entire protein structure, to open its active site for catalysis. This discovery of the molecular basis for the allosteric control of MltF catalysis is foundational to further study of MltF within the complex enzymatic orchestration of the dynamic peptidoglycan.
PubMed: 27618662
DOI: 10.1016/j.str.2016.07.019
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 5aa4
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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