1IW6
Crystal Structure of the Ground State of Bacteriorhodopsin
1IW6 の概要
| エントリーDOI | 10.2210/pdb1iw6/pdb |
| 関連するPDBエントリー | 1qm8 |
| 分子名称 | bacteriorhodopsin, beta-D-galactopyranose-(1-6)-alpha-D-mannopyranose-(1-2)-alpha-D-glucopyranose, RETINAL, ... (6 entities in total) |
| 機能のキーワード | 7 helix, riken structural genomics/proteomics initiative, rsgi, structural genomics, proton transport |
| 由来する生物種 | Halobacterium salinarum |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 31797.16 |
| 構造登録者 | Kouyama, T.,Okumura, H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2002-04-22, 公開日: 2002-12-11, 最終更新日: 2024-11-13) |
| 主引用文献 | Matsui, Y.,Sakai, K.,Murakami, M.,Shiro, Y.,Adachi, S.,Okumura, H.,Kouyama, T. Specific Damage Induced by X-ray Radiation and Structural Changes in the Primary Photoreaction of Bacteriorhodopsin. J.Mol.Biol., 324:469-481, 2002 Cited by PubMed Abstract: Bacteriorhodopsin, the sole membrane protein of the purple membrane of Halobacterium salinarum, functions as a light-driven proton pump. A 3-D crystal of bacteriorhodopsin, which was prepared by the membrane fusion method, was used to investigate structural changes in the primary photoreaction. It was observed that when a frozen crystal was exposed to a low flux of X-ray radiation (5 x 10(14)photons mm(-2)), nearly half of the protein was converted into an orange species, exhibiting absorption peaks at 450 nm, 478 nm and 510 nm. The remainder retained the normal photochemical activity until Asp85 in the active site was decarboxlyated by a higher flux of X-ray radiation (10(16)photons mm(-2)). The procedure of diffraction measurement was improved so as to minimize the effects of the radiation damage and determine the true structural change associated with the primary photoreaction. Our structural model of the K intermediate indicates that the Schiff base linkage and the adjacent bonds in the polyene chain of retinal are largely twisted so that the Schiff base nitrogen atom still interacts with a water molecule located near Asp85. With respect to the other part of the protein, no appreciable displacement is induced in the primary photoreaction. PubMed: 12445782DOI: 10.1016/S0022-2836(02)01110-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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