Stator assembly and activation mechanism of the flagellar motor by the periplasmic region of MotB

被引：127

作者：

Kojima, Seiji ^{[1
,2
]}

Imada, Katsumi ^{[1
,3
]}

Sakuma, Mayuko ^{[2
]}

Sudo, Yuki ^{[2
]}

Kojima, Chojiro ^{[4
]}

Minamino, Tohru ^{[1
,3
]}

Homma, Michio ^{[2
]}

Namba, Keiichi ^{[1
,3
]}

机构：

[1] Osaka Univ, Dynam NanoMachine Project, ICORP, JST, Suita, Osaka 5650871, Japan

[2] Nagoya Univ, Div Biol Sci, Grad Sch Sci, Chikusa Ku, Nagoya, Aichi 4648602, Japan

[3] Osaka Univ, Grad Sch Frontier Biosci, Suita, Osaka 5650871, Japan

[4] Nara Inst Sci & Technol, Biophys Lab, Grad Sch Biol Sci, Nara 6300192, Japan

来源：

MOLECULAR MICROBIOLOGY | 2009年 / 73卷 / 04期

关键词：

ESCHERICHIA-COLI; DELETION ANALYSIS; CRYSTAL-STRUCTURE; GENERATING UNITS; PROTEIN; MOTILITY; TORQUE; DOMAIN; COMPONENT; BACTERIA;

D O I：

10.1111/j.1365-2958.2009.06802.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 (MotBC) 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 MotBC are required both for PG binding and the proton channel activation.

引用

页码：710 / 718

页数：9

共 41 条

[11] BACTERIAL MOTILITY - MEMBRANE TOPOLOGY OF THE ESCHERICHIA-COLI MOTB PROTEIN [J].