4P02

Structure of Bacterial Cellulose Synthase with cyclic-di-GMP bound.

4P02 の概要

• エントリーDOI: 10.2210/pdb4p02/pdb
• 関連するPDBエントリー: 4HG6 4P00
• 分子名称: Cellulose Synthase subunit A, Cellulose Synthase subunit B, unidentified peptide, ... (8 entities in total)
• 機能のキーワード: membrane protein, allosteric activator, biofilm formation, cellulose biosynthesis, transferase
• 由来する生物種: Rhodobacter sphaeroides; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 174854.58

構造登録者

Morgan, J.L.W.,McNamara, J.T.,Zimmer, J. (登録日: 2014-02-20, 公開日: 2014-04-09, 最終更新日: 2023-12-27)

主引用文献

Morgan, J.L.,McNamara, J.T.,Zimmer, J.
Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP.
Nat.Struct.Mol.Biol., 21:489-496, 2014

PubMed Abstract: The bacterial signaling molecule cyclic di-GMP (c-di-GMP) stimulates the synthesis of bacterial cellulose, which is frequently found in biofilms. Bacterial cellulose is synthesized and translocated across the inner membrane by a complex of cellulose synthase BcsA and BcsB subunits. Here we present crystal structures of the c-di-GMP-activated BcsA-BcsB complex. The structures reveal that c-di-GMP releases an autoinhibited state of the enzyme by breaking a salt bridge that otherwise tethers a conserved gating loop that controls access to and substrate coordination at the active site. Disrupting the salt bridge by mutagenesis generates a constitutively active cellulose synthase. Additionally, the c-di-GMP-activated BcsA-BcsB complex contains a nascent cellulose polymer whose terminal glucose unit rests at a new location above BcsA's active site and is positioned for catalysis. Our mechanistic insights indicate how c-di-GMP allosterically modulates enzymatic functions.

PubMed: 24704788
DOI: 10.1038/nsmb.2803

実験手法

X-RAY DIFFRACTION (2.65 Å)