2VV5
The open structure of MscS
Summary for 2VV5
| Entry DOI | 10.2210/pdb2vv5/pdb |
| Descriptor | SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL (1 entity in total) |
| Functional Keywords | ion transport, transmembrane, inner membrane, membrane structure, membrane protein, membrane, transport, open channel, ionic channel |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cell inner membrane; Multi-pass membrane protein (By similarity): P0C0S2 |
| Total number of polymer chains | 7 |
| Total formula weight | 216656.67 |
| Authors | Wang, W.,Dong, C.,Johnson, K.A.,Naismith, J.H. (deposition date: 2008-06-03, release date: 2008-08-05, Last modification date: 2023-12-13) |
| Primary citation | Wang, W.,Black, S.S.,Edwards, M.D.,Miller, S.,Morrison, E.L.,Bartlett, W.,Dong, C.,Naismith, J.H.,Booth, I.R. The Structure of an Open Form of an E. Coli Mechanosensitive Channel at 3.45 A Resolution. Science, 321:1179-, 2008 Cited by PubMed Abstract: 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. PubMed: 18755969DOI: 10.1126/SCIENCE.1159262 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.45 Å) |
Structure validation
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