| Open and shut: Crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from E. coli and H. pylori at 4.4 Å and 4.1 Å resolution. | |
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MedLine Citation:
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PMID: 23339071 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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The mechanosensitive channel of small conductance (MscS) contributes to the survival of bacteria during osmotic downshock by transiently opening large diameter pores for the efflux of cellular contents before the membrane ruptures. Two crystal structures of the Escherichia coliMscS are currently available, the wild type protein in a non-conducting state at 3.7 Å resolution(Bass et al., Science 298, 1582 (2002)) and the Ala106Val variant in an open state at 3.45 Å resolution (Wang et al., Science 321, 1179 (2008)). Both structures used protein solubilized in the detergent fos-choline-14. We report here crystal structures of MscS from Escherichia coli and Helicobacter pylori solubilized in the detergent β-dodecylmaltoside (DDM) at resolutions of 4.4 and 4.2 Å, respectively. While the cytoplasmic domains are unchanged in these structures, distinctconformations of the transmembrane domains are observed. Intriguingly, DDM solubilized wild type E. coliMscSadopts the open state structure of A106V E. coliMscS, while H. pyloriMscS resembles the non-conducting state structure observed for fos-choline-14 solubilized E. coliMscS. These results highlight the sensitivity of membrane protein conformational equilibria to variationsin detergent, crystallization conditions and protein sequence. |
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Authors:
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Jeffrey Y Lai; Yan Shuen Poon; Jens T Kaiser; Douglas C Rees |
Publication Detail:
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Type: JOURNAL ARTICLE Date: 2013-1-22 |
Journal Detail:
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Title: Protein science : a publication of the Protein Society Volume: - ISSN: 1469-896X ISO Abbreviation: Protein Sci. Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-1-22 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9211750 Medline TA: Protein Sci Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2013 The Protein Society. |
Affiliation:
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Division of Chemistry and Chemical Engineering 114-96, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125. |
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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