The ATPase Motor Turns for Type IV Pilus Assembly

被引：9

作者：

Tsai, Chi-Lin ^{[1
]}

Tainer, John A. ^{[1
,2
]}

机构：

[1] Univ Texas MD Anderson Canc Ctr, Dept Mol & Cellular Oncol, Houston, TX 77030 USA

[2] Lawrence Berkeley Natl Lab, Mol Biophys & Integrated Bioimaging Div, Berkeley, CA 94720 USA

来源：

STRUCTURE | 2016年 / 24卷 / 11期

关键词：

RETRACTION MOTOR; PLATFORM PROTEIN; MOTILITY; BINDING;

D O I：

10.1016/j.str.2016.10.002

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：

In this issue of Structure, Mancl et al. (2016) elucidate the crystal structure of the PilB ATPase domain in complex with ATP gamma S and unveil how ATP binding and hydrolysis coordinates conformational change. Their results reveal a distinct symmetric rotary mechanism for ATP hydrolysis to power bacterial pilus assembly.

引用

页码：1857 / 1859

页数：3

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