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5EIY

Bacterial cellulose synthase bound to a substrate analogue

5EIY の概要
エントリーDOI10.2210/pdb5eiy/pdb
関連するPDBエントリー5EJ1 5EJZ
分子名称Putative cellulose synthase, [[(2~{R},3~{S},4~{R},5~{R})-5-[2,4-bis(oxidanylidene)pyrimidin-1-yl]-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-[[(2~{S},3~{R},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]methyl]phosphinic acid, poly(unk), ... (11 entities in total)
機能のキーワードcellulose biosynthesis, metal binding protein, membrane protein
由来する生物種Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
詳細
タンパク質・核酸の鎖数3
化学式量合計174032.32
構造登録者
McNamara, J.T.,Zimmer, J. (登録日: 2015-10-30, 公開日: 2016-03-09, 最終更新日: 2024-10-16)
主引用文献Morgan, J.L.,McNamara, J.T.,Fischer, M.,Rich, J.,Chen, H.M.,Withers, S.G.,Zimmer, J.
Observing cellulose biosynthesis and membrane translocation in crystallo.
Nature, 531:329-334, 2016
Cited by
PubMed Abstract: Many biopolymers, including polysaccharides, must be translocated across at least one membrane to reach their site of biological function. Cellulose is a linear glucose polymer synthesized and secreted by a membrane-integrated cellulose synthase. Here, in crystallo enzymology with the catalytically active bacterial cellulose synthase BcsA-BcsB complex reveals structural snapshots of a complete cellulose biosynthesis cycle, from substrate binding to polymer translocation. Substrate- and product-bound structures of BcsA provide the basis for substrate recognition and demonstrate the stepwise elongation of cellulose. Furthermore, the structural snapshots show that BcsA translocates cellulose via a ratcheting mechanism involving a 'finger helix' that contacts the polymer's terminal glucose. Cooperating with BcsA's gating loop, the finger helix moves 'up' and 'down' in response to substrate binding and polymer elongation, respectively, thereby pushing the elongated polymer into BcsA's transmembrane channel. This mechanism is validated experimentally by tethering BcsA's finger helix, which inhibits polymer translocation but not elongation.
PubMed: 26958837
DOI: 10.1038/nature16966
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.95 Å)
構造検証レポート
Validation report summary of 5eiy
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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