2VV5
The open structure of MscS
2VV5 の概要
エントリーDOI | 10.2210/pdb2vv5/pdb |
分子名称 | SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL (1 entity in total) |
機能のキーワード | ion transport, transmembrane, inner membrane, membrane structure, membrane protein, membrane, transport, open channel, ionic channel |
由来する生物種 | ESCHERICHIA COLI |
細胞内の位置 | Cell inner membrane; Multi-pass membrane protein (By similarity): P0C0S2 |
タンパク質・核酸の鎖数 | 7 |
化学式量合計 | 216656.67 |
構造登録者 | Wang, W.,Dong, C.,Johnson, K.A.,Naismith, J.H. (登録日: 2008-06-03, 公開日: 2008-08-05, 最終更新日: 2023-12-13) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.45 Å) |
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