The structure of an open form of an E. coli mechanosensitive channel at 3.45A resolution

Wenjian Wang; Susan S. Black; Michelle D. Edwards; Samantha Miller; Emma L. Morrison; Wendy Bartlett; Changjiang Dong; James H. Naismith; Ian R. Booth

doi:10.1126/science.1159262

The structure of an open form of an E. coli mechanosensitive channel at 3.45A resolution

Wenjian Wang, Susan S. Black, Michelle D. Edwards, Samantha Miller, Emma L. Morrison, Wendy Bartlett, Changjiang Dong, James H. Naismith, Ian R. Booth

Research output: Contribution to journal › Article › peer-review

174 Citations (Scopus)

Abstract

How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia 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 angstrom-resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of ~13 angstroms created by substantial rotational rearrangement 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.

Original language	English
Pages (from-to)	1179-1183
Number of pages	5
Journal	Science
Volume	321
Issue number	5893
DOIs	https://doi.org/10.1126/science.1159262
Publication status	Published - 29 Aug 2008

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10.1126/science.1159262

Cite this

@article{c2b81f70f9c24d929657720401cc9a35,

title = "The structure of an open form of an E. coli mechanosensitive channel at 3.45A resolution",

abstract = "How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia 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 angstrom-resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of ~13 angstroms created by substantial rotational rearrangement 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.",

author = "Wenjian Wang and Black, {Susan S.} and Edwards, {Michelle D.} and Samantha Miller and Morrison, {Emma L.} and Wendy Bartlett and Changjiang Dong and Naismith, {James H.} and Booth, {Ian R.}",

year = "2008",

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doi = "10.1126/science.1159262",

language = "English",

volume = "321",

pages = "1179--1183",

journal = "Science",

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TY - JOUR

T1 - The structure of an open form of an E. coli mechanosensitive channel at 3.45A resolution

AU - Wang, Wenjian

AU - Black, Susan S.

AU - Edwards, Michelle D.

AU - Miller, Samantha

AU - Morrison, Emma L.

AU - Bartlett, Wendy

AU - Dong, Changjiang

AU - Naismith, James H.

AU - Booth, Ian R.

PY - 2008/8/29

Y1 - 2008/8/29

N2 - How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia 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 angstrom-resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of ~13 angstroms created by substantial rotational rearrangement 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.

AB - How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia 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 angstrom-resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of ~13 angstroms created by substantial rotational rearrangement 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.

U2 - 10.1126/science.1159262

DO - 10.1126/science.1159262

M3 - Article

VL - 321

SP - 1179

EP - 1183

JO - Science

JF - Science

SN - 0036-8075

IS - 5893

ER -