期刊
STRUCTURE
卷 17, 期 6, 页码 893-903出版社
CELL PRESS
DOI: 10.1016/j.str.2009.03.018
关键词
-
资金
- Department of Energy, Office of Biological and Environmental Research
- INBRE Program of the NCRR [P20 RR-016464]
- Wellcome Trust [GR040174, 065268]
- Medical Research Council [G0400277] Funding Source: researchfish
- MRC [G0400277] Funding Source: UKRI
KTN (RCK) domains are nucleotide-binding folds that form the cytoplasmic regulatory complexes of various K+ channels and transporters. The mechanisms these proteins use to control their transmembrane pore-forming counterparts remains unclear despite numerous electrophysiological and structural studies. KTN (RCK) domains consistently crystallize as dimers within the asymmetric unit, forming a pronounced hinge between two Rossmann folds. We have previously proposed that modification of the hinge angle plays an important role in activating the associated membrane-integrated components of the channel or transporter. Here we report the structure of the C-terminal, KTN-bearing domain of the E. coli KefC K+ efflux system in association with the ancillary subunit, KefF, which is known to stabilize the conductive state. The structure of the complex and functional analysis of KefC variants reveal that control of the conformational flexibility inherent in the KTN dimer hinge is modulated by KefF and essential for regulation of KefC ion flux.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据