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

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 av...

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Bibliographic Details
Published in:Protein science 2013-04, Vol.22 (4), p.502-509
Main Authors: Lai, Jeffrey Y., Poon, Yan Shuen, Kaiser, Jens T., Rees, Douglas C.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Bacterial Proteins - chemistry
Crystallography, X-Ray
Detergents - chemistry
Escherichia coli - chemistry
Escherichia coli - metabolism
Escherichia coli Proteins - chemistry
For the Record
Glucosides - chemistry
Helicobacter pylori - chemistry
Helicobacter pylori - metabolism
Ion Channels - chemistry
mechanosensitive channel
membrane protein structure
Models, Molecular
Molecular Sequence Data
MscS
Protein Conformation
protein structure
Recombinant Proteins - chemistry
Sequence Alignment
Solubility
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Summary: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. Interactive View | PDB Code(s): 4HWA, 4HW9
ISSN:0961-8368
1469-896X
DOI:10.1002/pro.2222