The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution.
The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution.
复制标题
DOI:
10.1126/science.1159262
复制
发表时间:
2008-08-29
期刊:
影响因子:
--
通讯作者:
Booth IR
中科院分区:
文献类型:
--
作者:
Wang W;Black SS;Edwards MD;Miller S;Morrison EL;Bartlett W;Dong C;Naismith JH;Booth IR
How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The E. coli mechanosensitive channel, MscS, opens to allow rapid ion efflux, relieving the turgor pressure that would otherwise destroy the cell. We present a 3.45 Å resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of ~13 Å created by substantial rotational re-arrangement of the three transmembrane helices. The structure suggests a molecular mechanism that underlies MscS gating and its decay of conductivity during prolonged activation. Support for this mechanism is provided by single channel analysis of mutants with altered gating characteristics.
登录
查看更多内容
影响因子:
64.8
作者:
Long, Stephen B.;Tao, Xiao;MacKinnon, Roderick
通讯作者:
MacKinnon, Roderick
影响因子:
64.5
作者:
CARTER, PJ;WINTER, G;FERSHT, AR
通讯作者:
FERSHT, AR
影响因子:
16.8
作者:
Edwards, MD;Li, YZ;Booth, IR
通讯作者:
Booth, IR
DOI:
10.1085/jgp.200409198
发表时间:
2005-02
期刊:
The Journal of general physiology
影响因子:
--
作者:
Akitake B;Anishkin A;Sukharev S
通讯作者:
Sukharev S
影响因子:
56.9
作者:
Long, SB;Campbell, EB;MacKinnon, R
通讯作者:
MacKinnon, R