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.
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DOI:
10.1126/science.1159262
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发表时间:
2008-08-29
期刊:
Science (New York, N.Y.)
影响因子:
--
通讯作者:
Booth IR
Booth IR
中科院分区:
其他
文献类型:
--
作者:
Wang W;Black SS;Edwards MD;Miller S;Morrison EL;Bartlett W;Dong C;Naismith JH;Booth IR

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离子通道如何被门控以调节进出细胞的离子通量是人们非常感兴趣的课题。大肠杆菌的机械敏感通道MscS打开,允许离子快速流出,减轻肿胀压力,否则会破坏细胞。我们提出了一个3.45 Å分辨率结构的MscS通道在一个开放的构象。该结构的孔径为~13 Å,这是由三个跨膜螺旋的大量旋转重新排列产生的。该结构提示了MscS门控及其在长时间激活过程中电导率衰减的分子机制。支持这一机制的是对具有改变的门控特性的突变体的单通道分析。
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.
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