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
收藏
页码：1857 / 1859
页数：3
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