Linked Life Data

12767977

Source:http://linkedlifedata.com/resource/pubmed/id/12767977

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pubmed-article:12767977pubmed:abstractTextMechanosensitive channels must make a large conformational change during the transition from the closed to the open state. The crystal structure of the open form of the Escherichia coli MscS channel was recently solved and depicts a homoheptamer (1). In this study, cross-linking of site-specific cysteine substitutions demonstrates that residues up to 10-33 A apart in the crystal structure readily form disulfide bridges in the closed form and can also be cross-linked by a 10-A linker. Cross-linking between adjacent subunits stabilizes the heptameric form of the channel providing biochemical evidence to support the crystal structure. The data are consistent with the published model (1) in that the membrane domain is highly flexible and that the closed to open transition may involve a significant displacement of transmembrane helices 1 and 2, possibly by as much as 30 A. The data are also consistent with significant flexibility of the cytoplasmic domain.lld:pubmed
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pubmed-article:12767977pubmed:articleTitleThe closed structure of the MscS mechanosensitive channel. Cross-linking of single cysteine mutants.lld:pubmed
pubmed-article:12767977pubmed:affiliationDepartment of Molecular & Cell Biology, Institute of Medical Sciences, University of Aberdeen, Foresterhill, Aberdeen AB25 2ZD, United Kingdom.lld:pubmed
pubmed-article:12767977pubmed:publicationTypeJournal Articlelld:pubmed
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