1PRC
CRYSTALLOGRAPHIC REFINEMENT AT 2.3 ANGSTROMS RESOLUTION AND REFINED MODEL OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS
1PRC の概要
| エントリーDOI | 10.2210/pdb1prc/pdb |
| 分子名称 | PHOTOSYNTHETIC REACTION CENTER, SULFATE ION, MENAQUINONE-7, ... (14 entities in total) |
| 機能のキーワード | photosynthetic reaction center |
| 由来する生物種 | Blastochloris viridis 詳細 |
| 細胞内の位置 | Cell membrane; Lipid-anchor: P07173 Cellular chromatophore membrane; Multi-pass membrane protein (By similarity): P06009 P06010 Cellular chromatophore membrane; Single-pass membrane protein: P06008 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 142923.19 |
| 構造登録者 | Deisenhofer, J.,Epp, O.,Miki, K.,Huber, R.,Michel, H. (登録日: 1988-02-04, 公開日: 1989-01-09, 最終更新日: 2024-10-16) |
| 主引用文献 | Deisenhofer, J.,Epp, O.,Sinning, I.,Michel, H. Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis. J.Mol.Biol., 246:429-457, 1995 Cited by PubMed Abstract: The atomic model of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis has been refined to an R-value of 0.193 at 2.3 A resolution. The refined model contains 10,288 non-hydrogen atoms; 10,045 of these have well defined electron density. A Luzzati-plot indicates an average co-ordinate error of 0.26 A. During refinement, the positions of a partially ordered carotenoid, a unibiquinone in the partially occupied QB site, a detergent molecule, seven putative sulphate ions, and 201 water molecules were found. More than half of these waters are bound at interfaces between protein subunits and therefore contribute significantly to subunit interactions. Water molecules also play important structural and probably functional roles in the environment of some of the cofactors. Two water molecules form hydrogen bonds to the accessory bacteriochlorophylls and to the protein in the vicinity of the special pair of bacteriophylls, the primary electron donor. A group of about 10 water molecules is bound near the binding site of the secondary quinone QB. These waters are likely to participate in the transfer of protons to the doubly reduced QB. PubMed: 7877166DOI: 10.1006/jmbi.1994.0097 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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