1QHJ
X-RAY STRUCTURE OF BACTERIORHODOPSIN GROWN IN LIPIDIC CUBIC PHASES
1QHJ の概要
エントリーDOI | 10.2210/pdb1qhj/pdb |
分子名称 | PROTEIN (BACTERIORHODOPSIN), RETINAL, 1,2-[DI-2,6,10,14-TETRAMETHYL-HEXADECAN-16-OXY]-PROPANE, ... (4 entities in total) |
機能のキーワード | photoreceptor, proton pump, membrane protein, retinal protein, lipidic cubic phases, purple membrane, archeal lipids |
由来する生物種 | Halobacterium salinarum |
細胞内の位置 | Cell membrane; Multi-pass membrane protein: P02945 |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 32833.27 |
構造登録者 | Belrhali, H.,Nollert, P.,Royant, A.,Menzel, C.,Rosenbusch, J.P.,Landau, E.M.,Pebay-Peyroula, E. (登録日: 1999-05-04, 公開日: 1999-07-21, 最終更新日: 2024-10-30) |
主引用文献 | Belrhali, H.,Nollert, P.,Royant, A.,Menzel, C.,Rosenbusch, J.P.,Landau, E.M.,Pebay-Peyroula, E. Protein, lipid and water organization in bacteriorhodopsin crystals: a molecular view of the purple membrane at 1.9 A resolution. Structure Fold.Des., 7:909-917, 1999 Cited by PubMed Abstract: Bacteriorhodopsin (bR) from Halobacterium salinarum is a proton pump that converts the energy of light into a proton gradient that drives ATP synthesis. The protein comprises seven transmembrane helices and in vivo is organized into purple patches, in which bR and lipids form a crystalline two-dimensional array. Upon absorption of a photon, retinal, which is covalently bound to Lys216 via a Schiff base, is isomerized to a 13-cis,15-anti configuration. This initiates a sequence of events - the photocycle - during which a proton is transferred from the Schiff base to Asp85, followed by proton release into the extracellular medium and reprotonation from the cytoplasmic side. PubMed: 10467143DOI: 10.1016/S0969-2126(99)80118-X 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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