4RCR
STRUCTURE OF THE REACTION CENTER FROM RHODOBACTER SPHAEROIDES R-26 AND 2.4.1: PROTEIN-COFACTOR (BACTERIOCHLOROPHYLL, BACTERIOPHEOPHYTIN, AND CAROTENOID) INTERACTIONS
4RCR の概要
| エントリーDOI | 10.2210/pdb4rcr/pdb |
| 分子名称 | PHOTOSYNTHETIC REACTION CENTER, BACTERIOCHLOROPHYLL A, BACTERIOPHEOPHYTIN A, ... (8 entities in total) |
| 機能のキーワード | photosynthetic reaction center |
| 由来する生物種 | Rhodobacter sphaeroides 詳細 |
| 細胞内の位置 | Cellular chromatophore membrane; Multi-pass membrane protein: P02954 P02953 Cellular chromatophore membrane; Single-pass membrane protein: P11846 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 101310.60 |
| 構造登録者 | Komiya, H.,Yeates, T.O.,Chirino, A.J.,Rees, D.C.,Allen, J.P.,Feher, G. (登録日: 1991-09-09, 公開日: 1993-10-31, 最終更新日: 2024-12-25) |
| 主引用文献 | Yeates, T.O.,Komiya, H.,Chirino, A.,Rees, D.C.,Allen, J.P.,Feher, G. Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: protein-cofactor (bacteriochlorophyll, bacteriopheophytin, and carotenoid) interactions. Proc.Natl.Acad.Sci.USA, 85:7993-7997, 1988 Cited by PubMed Abstract: The three-dimensional structures of the cofactors and protein subunits of the reaction center (RC) from the carotenoidless mutant strain of Rhodobacter sphaeroides R-26 and the wild-type strain 2.4.1 have been determined by x-ray diffraction to resolutions of 2.8 A and 3.0 A with R values of 24% and 26%, respectively. The bacteriochlorophyll dimer (D), bacteriochlorophyll monomers (B), and bacteriopheophytin monomers (phi) form two branches, A and B, that are approximately related by a twofold symmetry axis. The cofactors are located in hydrophobic environments formed by the L and M subunits. Differences in the cofactor-protein interactions between the A and B cofactors, as well as between the corresponding cofactors of Rb, sphaeroides and Rhodopseudomonas viridis [Michel, H., Epp, O. & Deisenhofer, J. (1986) EMBO J. 3, 2445-2451], are delineated. The roles of several structural features in the preferential electron transfer along the A branch are discussed. Two bound detergent molecules of beta-octyl glucoside have been located near BA and BB. The environment of the carotenoid, C, that is present in RCs from Rb. sphaeroides 2.4.1 consists largely of aromatic residues of the M subunit. A role of BB in the triplet energy transfer from D to C and the reason for the preferential ease of removal of BB from the RC is proposed. PubMed: 3186702DOI: 10.1073/pnas.85.21.7993 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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