2ZOV

Structure of the periplasmic domain of MotB from Salmonella (crystal form I)

2ZOV の概要

• エントリーDOI: 10.2210/pdb2zov/pdb
• 関連するPDBエントリー: 2zvy 2zvz
• 分子名称: Chemotaxis protein motB (2 entities in total)
• 機能のキーワード: 2-layer sandwich, bacterial flagellum, cell projection, chemotaxis, flagellar rotation, inner membrane, membrane, transmembrane, membrane protein
• 由来する生物種: Salmonella typhimurium
• 細胞内の位置: Cell inner membrane (By similarity); Single- pass type II membrane protein (Potential): P55892
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 23982.19

構造登録者

Imada, K.,Kojima, S.,Namba, K.,Homma, M. (登録日: 2008-06-09, 公開日: 2009-06-09, 最終更新日: 2024-11-06)

主引用文献

Kojima, S.,Imada, K.,Sakuma, M.,Sudo, Y.,Kojima, C.,Minamino, T.,Homma, M.,Namba, K.
Stator assembly and activation mechanism of the flagellar motor by the periplasmic region of MotB
Mol.Microbiol., 73:710-718, 2009

PubMed Abstract: Torque generation in the Salmonella flagellar motor is coupled to translocation of H(+) ions through the proton-conducting channel of the Mot protein stator complex. The Mot complex is believed to be anchored to the peptidoglycan (PG) layer by the putative peptidoglycan-binding (PGB) domain of MotB. Proton translocation is activated only when the stator is installed into the motor. We report the crystal structure of a C-terminal periplasmic fragment of MotB (MotB(C)) that contains the PGB domain and includes the entire periplasmic region essential for motility. Structural and functional analyses indicate that the PGB domains must dimerize in order to form the proton-conducting channel. Drastic conformational changes in the N-terminal portion of MotB(C) are required both for PG binding and the proton channel activation.

PubMed: 19627504
DOI: 10.1111/j.1365-2958.2009.06802.x

実験手法

X-RAY DIFFRACTION (2 Å)