The Structure of an Open Form of an E. coli Mechanosensitive Channel at 3.45 Å Resolution-Reference-Cited by-同舟云学术

The Structure of an Open Form of an E. coli Mechanosensitive Channel at 3.45 Å Resolution

Published:2008-08-29 Issue:5893 Volume:321 Page:1179-1183
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Wang Wenjian¹²,Black Susan S.¹²,Edwards Michelle D.¹²,Miller Samantha¹²,Morrison Emma L.¹²,Bartlett Wendy¹²,Dong Changjiang¹²,Naismith James H.¹²,Booth Ian R.¹²

Affiliation:

1. Centre for Biomolecular Sciences, The North Haugh, University of St. Andrews, KY16 9ST, Scotland, UK.

2. School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, Scotland, UK.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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