ArticleProtein science : a publication of the Protein Society2013
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.
Article in Protein science : a publication of the Protein Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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41 citing papers in PubMed.
- The diverse gating mechanisms of bacterial MscS-like ion channels.Biochemical Society transactions · 2026Review
- Structural Specificity of Polymorphic Forms of α-Synuclein Amyloid.Biomedicines · 2023Article
- How Functional Lipids Affect the Structure and Gating of Mechanosensitive MscS-like Channels.International journal of molecular sciences · 2022Review
- Root osmotic sensing from local perception to systemic responses.Stress biology · 2022Review
- Roles of Bacterial Mechanosensitive Channels in Infection and Antibiotic Susceptibility.Pharmaceuticals (Basel, Switzerland) · 2022Review
- Structural insights into the Venus flytrap mechanosensitive ion channel Flycatcher1.Nature communications · 2022Article
- Dependence of Protein Structure on Environment: FOD Model Applied to Membrane Proteins.Membranes · 2021Article
- Mechanosensitive channel gating by delipidation.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Mechanosensitive channel YnaI has lipid-bound extended sensor paddles.Communications biology · 2021Article
- Model of Environmental Membrane Field for Transmembrane Proteins.International journal of molecular sciences · 2021Article
- Article
- Cyclodextrins for structural and functional studies of mechanosensitive channels.Journal of structural biology: X · 2021Article
- Charged pore-lining residues are required for normal channel kinetics in the eukaryotic mechanosensitive ion channel MSL1.Channels (Austin, Tex.) · 2020Article
- The MscS-like channel YnaI has a gating mechanism based on flexible pore helices.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural mechanism for gating of a eukaryotic mechanosensitive channel of small conductance.Nature communications · 2020Article
- In-Lipid Structure of Pressure-Sensitive Domains Hints Mechanosensitive Channel Functional Diversity.Biophysical journal · 2020Article
- Life with Bacterial Mechanosensitive Channels, from Discovery to Physiology to Pharmacological Target.Microbiology and molecular biology reviews : MMBR · 2020Review
- Article
- Allosteric activation of an ion channel triggered by modification of mechanosensitive nano-pockets.Nature communications · 2019Article
- Nonpolar residues in the presumptive pore-lining helix of mechanosensitive channel MSL10 influence channel behavior and establish a nonconducting function.Plant direct · 2018Article
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4 authors.
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Abstract
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.
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