5AJI
MscS D67R1 high resolution
5AJI の概要
| エントリーDOI | 10.2210/pdb5aji/pdb |
| 関連するPDBエントリー | 5AIT 5AIU |
| 分子名称 | SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL, N-OCTANE, HEXANE, ... (4 entities in total) |
| 機能のキーワード | transport protein |
| 由来する生物種 | ESCHERICHIA COLI |
| 細胞内の位置 | Cell inner membrane ; Multi- pass membrane protein : P0C0S2 |
| タンパク質・核酸の鎖数 | 7 |
| 化学式量合計 | 219183.69 |
| 構造登録者 | |
| 主引用文献 | Pliotas, C.,Dahl, A.C.E.,Rasmussen, T.,Mahendran, K.R.,Smith, T.K.,Marius, P.,Gault, J.,Banda, T.,Rasmussen, A.,Miller, S.,Robinson, C.V.,Bayley, H.,Sansom, M.S.P.,Booth, I.R.,Naismith, J.H. The Role of Lipids in Mechanosensation. Nat.Struct.Mol.Biol., 22:991-, 2015 Cited by PubMed Abstract: The ability of proteins to sense membrane tension is pervasive in biology. A higher-resolution structure of the Escherichia coli small-conductance mechanosensitive channel MscS identifies alkyl chains inside pockets formed by the transmembrane helices (TMs). Purified MscS contains E. coli lipids, and fluorescence quenching demonstrates that phospholipid acyl chains exchange between bilayer and TM pockets. Molecular dynamics and biophysical analyses show that the volume of the pockets and thus the number of lipid acyl chains within them decreases upon channel opening. Phospholipids with one acyl chain per head group (lysolipids) displace normal phospholipids (with two acyl chains) from MscS pockets and trigger channel opening. We propose that the extent of acyl-chain interdigitation in these pockets determines the conformation of MscS. When interdigitation is perturbed by increased membrane tension or by lysolipids, the closed state becomes unstable, and the channel gates. PubMed: 26551077DOI: 10.1038/NSMB.3120 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.99 Å) |
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