2vv5

The open structure of MscS

spinqualitylabelsall models 2vv5, resolution 3.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vv5 is a 7 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. The November 2008 RCSB PDB Molecule of the Month feature on Mechanosensitive Channels by David Goodsell is 10.2210/rcsb_pdb/mom_2008_11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [MSCS_ECO57] Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell. Forms an ion channel of 1.0 nanosiemens conductance with a slight preference for anions. The channel is sensitive to voltage (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed How ion channels are gated to regulate ion flux in and out of cells is the subject of intense interest. The Escherichia coli mechanosensitive channel, MscS, opens to allow rapid ion efflux, relieving the turgor pressure that would otherwise destroy the cell. We present a 3.45 angstrom-resolution structure for the MscS channel in an open conformation. This structure has a pore diameter of approximately 13 angstroms created by substantial rotational rearrangement of the three transmembrane helices. The structure suggests a molecular mechanism that underlies MscS gating and its decay of conductivity during prolonged activation. Support for this mechanism is provided by single-channel analysis of mutants with altered gating characteristics. The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution.,Wang W, Black SS, Edwards MD, Miller S, Morrison EL, Bartlett W, Dong C, Naismith JH, Booth IR Science. 2008 Aug 29;321(5893):1179-83. PMID:18755969 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ion channels Mechanosensitive channels: opening and closing

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