High-resolution structure of the open NaK channel.
High-resolution structure of the open NaK channel.
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DOI:
10.1038/nsmb.1531
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发表时间:
2009-01
影响因子:
16.8
通讯作者:
中科院分区:
文献类型:
--
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We report the crystal structure of the non-selective cation channel NaK from b. cereus at a resolution of 1.6 Å. The structure reveals the intracellular gate in an open state compared to the closed form reported previously, making NaK the only channel for which the three-dimensional structures of both conformations are known. Channel opening follows a conserved mechanism of inner helix bending utilizing a flexible glycine residue, the gating hinge, seen in MthK and most other tetrameric cation channels. Additionally, distinct inter and intra-subunit rearrangements involved in channel gating are seen and characterized for the first time along with inner helix twisting motions. Furthermore, we identify a residue deeper within the cavity of the channel pore, Phe92, which likely forms a constriction point within the open pore, restricting ion flux through the channel. Mutating this residue to Ala causes a subsequent increase in ion conduction rates as measured by 86Rb flux assays. The structures of both the open and closed conformations of the NaK channel correlate very well with those of equivalent K+ channel conformations, namely MthK and KcsA, respectively.
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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:
56.9
作者:
Doyle, DA;Cabral, JM;MacKinnon, R
通讯作者:
MacKinnon, R
影响因子:
3.8
作者:
Ding, Shinghua;Ingleby, Lindsey;Ahern, Christopher A;Horn, Richard
通讯作者:
Horn, Richard
DOI:
10.1073/pnas.92.18.8239
发表时间:
1995-08-29
影响因子:
11.1
作者:
RABENSTEIN, MD;SHIN, YK
通讯作者:
SHIN, YK
DOI:
10.1085/jgp.114.4.551
发表时间:
1999-10
期刊:
The Journal of general physiology
影响因子:
--
作者:
Heginbotham L;LeMasurier M;Kolmakova-Partensky L;Miller C
通讯作者:
Miller C