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

Wenjian Wang; Susan Shirley Black; Michelle D. Edwards; Samantha Miller; Emma Louise 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 3.45 Å resolution

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

Medical Sciences

University of St Andrews

Research output: Contribution to journal › Article

172 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 similar to 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

Keywords

gated potassium channel
acetylcholine-receptor
crystal-structure
ion-channel
K+ channel
protein stability
MSCS
pore
mechanism
cooperativity

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10.1126/science.1159262

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title = "The structure of an open form of an E. coli mechanosensitive channel at 3.45 {\AA} 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 similar to 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.",

keywords = "gated potassium channel, acetylcholine-receptor, crystal-structure, ion-channel, K+ channel, protein stability, MSCS, pore, mechanism, cooperativity",

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

year = "2008",

month = aug,

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doi = "10.1126/science.1159262",

language = "English",

volume = "321",

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TY - JOUR

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

AU - Wang, Wenjian

AU - Black, Susan Shirley

AU - Edwards, Michelle D.

AU - Miller, Samantha

AU - Morrison, Emma Louise

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 similar to 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 similar to 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.

KW - gated potassium channel

KW - acetylcholine-receptor

KW - crystal-structure

KW - ion-channel

KW - K+ channel

KW - protein stability

KW - MSCS

KW - pore

KW - mechanism

KW - cooperativity

U2 - 10.1126/science.1159262

DO - 10.1126/science.1159262

M3 - Article

SN - 0036-8075

VL - 321

SP - 1179

EP - 1183

JO - Science

JF - Science

IS - 5893

ER -

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

Abstract

Keywords

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