Document Detail

Open and shut: crystal structures of the dodecylmaltoside solubilized mechanosensitive channel of small conductance from Escherichia coli and Helicobacter pylori at 4.4 Å and 4.1 Å resolutions.
MedLine Citation:
PMID:  23339071     Owner:  NLM     Status:  MEDLINE    
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 coli MscS are currently available, the wild type protein in a nonconducting state at 3.7 Å resolution (Bass et al., Science 2002; 298:1582-1587) and the Ala106Val variant in an open state at 3.45 Å resolution (Wang et al., Science 2008; 321:1179-1183). Both structures used protein solubilized in the detergent fos-choline-14. We report here crystal structures of MscS from E. coli and Helicobacter pylori solubilized in the detergent β-dodecylmaltoside at resolutions of 4.4 and 4.2 Å, respectively. While the cytoplasmic domains are unchanged in these structures, distinct conformations of the transmembrane domains are observed. Intriguingly, β-dodecylmaltoside solubilized wild type E. coli MscS adopts the open state structure of A106V E. coli MscS, while H. pylori MscS resembles the nonconducting state structure observed for fos-choline-14 solubilized E. coli MscS. These results highlight the sensitivity of membrane protein conformational equilibria to variations in detergent, crystallization conditions, and protein sequence.
Jeffrey Y Lai; Yan Shuen Poon; Jens T Kaiser; Douglas C Rees
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2013-02-21
Journal Detail:
Title:  Protein science : a publication of the Protein Society     Volume:  22     ISSN:  1469-896X     ISO Abbreviation:  Protein Sci.     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-03-20     Completed Date:  2013-08-26     Revised Date:  2014-07-04    
Medline Journal Info:
Nlm Unique ID:  9211750     Medline TA:  Protein Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  502-9     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 The Protein Society.
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MeSH Terms
Amino Acid Sequence
Bacterial Proteins / chemistry*
Crystallography, X-Ray
Detergents / chemistry
Escherichia coli / chemistry*,  metabolism
Escherichia coli Proteins / chemistry*
Glucosides / chemistry
Helicobacter pylori / chemistry*,  metabolism
Ion Channels / chemistry*
Models, Molecular
Molecular Sequence Data
Protein Conformation
Recombinant Proteins / chemistry
Sequence Alignment
Grant Support
Reg. No./Substance:
0/Bacterial Proteins; 0/Detergents; 0/Escherichia coli Proteins; 0/Glucosides; 0/Ion Channels; 0/MscS protein, E coli; 0/Recombinant Proteins; 69227-93-6/dodecyl maltoside

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