Structure of an Open Form of an E. coli Mechanosensitive Channel at 3.45 Å Resolution
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 str...
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| Published in | Science (American Association for the Advancement of Science) Vol. 321; no. 5893; pp. 1179 - 1183 |
|---|---|
| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Washington, DC
American Association for the Advancement of Science
29.08.2008
|
| Subjects | |
| Online Access | Get full text |
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| 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. |
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| AbstractList | 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. 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 approximately 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. 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. 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 approximately 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.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 approximately 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. 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 613 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. 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 | Black, Susan S Morrison, Emma L Miller, Samantha Naismith, James H Booth, Ian R Edwards, Michelle D Dong, Changjiang Wang, Wenjian Bartlett, Wendy |
| AuthorAffiliation | 2 School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, UK 3 Centre for Biomolecular Sciences, The North Haugh, The University, St Andrews, KY16 9ST, UK |
| AuthorAffiliation_xml | – name: 2 School of Medical Sciences, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen, AB25 2ZD, UK – name: 3 Centre for Biomolecular Sciences, The North Haugh, The University, St Andrews, KY16 9ST, UK |
| Author_xml | – sequence: 1 fullname: Wang, Wenjian – sequence: 2 fullname: Black, Susan S – sequence: 3 fullname: Edwards, Michelle D – sequence: 4 fullname: Miller, Samantha – sequence: 5 fullname: Morrison, Emma L – sequence: 6 fullname: Bartlett, Wendy – sequence: 7 fullname: Dong, Changjiang – sequence: 8 fullname: Naismith, James H – sequence: 9 fullname: Booth, Ian R |
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| Snippet | 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,... 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,... 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... |
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| SubjectTerms | Biological and medical sciences Cell Membrane - chemistry Crystal structure Crystallography, X-Ray Electric Conductivity Escherichia coli Escherichia coli - chemistry Escherichia coli - physiology Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - physiology Free energy Fundamental and applied biological sciences. Psychology Hydrophobic and Hydrophilic Interactions Ion Channel Gating Ion channels Ion Channels - chemistry Ion Channels - genetics Ion Channels - physiology Kinetics Microbiology Modeling Models, Molecular Molecules Monomers Morphology, structure, chemical composition, physicochemical properties Mutant Proteins - chemistry mutants Mutation P branes Patch-Clamp Techniques Pressure Protein Conformation Protein Structure, Secondary Protein Structure, Tertiary Research Article String theory turgor Vapors Virology |
| Title | Structure of an Open Form of an E. coli Mechanosensitive Channel at 3.45 Å Resolution |
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