5Y40

Structure of the periplasmic domain of the MotB L119P mutant from Salmonella (crystal form 2)

5Y40 の概要

• エントリーDOI: 10.2210/pdb5y40/pdb
• 関連するPDBエントリー: 2ZOV 2ZVY 2ZVZ 5Y3Z
• 分子名称: Motility protein B (1 entity in total)
• 機能のキーワード: 2-layer sandwich, bacterial flagellum, cell projection, chemotaxis, flagellar rotation, inner membrane, membrane protein, motor protein
• 由来する生物種: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
• 細胞内の位置: Cell inner membrane ; Single- pass type II membrane protein : P55892
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 82874.52

構造登録者

Takao, M.,Kojima, S.,Sakuma, M.,Homma, M.,Imada, K. (登録日: 2017-07-31, 公開日: 2018-04-11, 最終更新日: 2023-11-22)

主引用文献

Kojima, S.,Takao, M.,Almira, G.,Kawahara, I.,Sakuma, M.,Homma, M.,Kojima, C.,Imada, K.
The Helix Rearrangement in the Periplasmic Domain of the Flagellar Stator B Subunit Activates Peptidoglycan Binding and Ion Influx.
Structure, 26:590-598.e5, 2018

PubMed Abstract: The stator of the bacterial flagellar motor couples ion flow with torque generation. The ion-conducting stator channel opens only when incorporated into and anchored around the rotor via the peptidoglycan (PG) binding domain of the B subunit (MotB). However, no direct evidence of PG binding coupled with channel activation has been presented. Here, we report the structural rearrangements of MotB responsible for this coupling process. A MotB fragment with the L119P replacement, which is known to cause channel activation, was able to bind PG. Nuclear magnetic resonance analysis of MotB and the crystal structure of the MotB-L119P dimer revealed major structural changes in helix α1. In vivo crosslinking results confirm that a major rearrangement occurs. Our results suggest that, upon stator incorporation into the motor, helix α1 of MotB changes into an extended non-helical structure. We propose that this change allows the stator both to bind PG and to open its proton channel.

PubMed: 29576320
DOI: 10.1016/j.str.2018.02.016

実験手法

X-RAY DIFFRACTION (2.8 Å)