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1RG5

Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides carotenoidless strain R-26.1

1RG5 の概要
エントリーDOI10.2210/pdb1rg5/pdb
関連するPDBエントリー1rgn 1rqk 4rcr
分子名称Reaction center protein L chain, LAURYL DIMETHYLAMINE-N-OXIDE, Reaction center protein M chain, ... (11 entities in total)
機能のキーワードphotosynthesis, photosynthetic reaction center, carotenoidless mutant, carotenoid binding site, membrane protein
由来する生物種Rhodobacter sphaeroides
詳細
タンパク質・核酸の鎖数3
化学式量合計104155.09
構造登録者
Roszak, A.W.,Hashimoto, H.,Gardiner, A.T.,Cogdell, R.J.,Isaacs, N.W. (登録日: 2003-11-11, 公開日: 2004-04-27, 最終更新日: 2024-02-14)
主引用文献Roszak, A.W.,McKendrick, K.,Gardiner, A.T.,Mitchell, I.A.,Isaacs, N.W.,Cogdell, R.J.,Hashimoto, H.,Frank, H.A.
Protein Regulation of Carotenoid Binding: Gatekeeper and Locking Amino Acid Residues in Reaction Centers of Rhodobacter sphaeroides
STRUCTURE, 12:765-773, 2004
Cited by
PubMed Abstract: X-ray diffraction was used to determine high-resolution structures of the reaction center (RC) complex from the carotenoidless mutant, Rb. sphaeroides R-26.1, without or reconstituted with carotenoids. The results are compared with the structure of the RC from a semiaerobically grown Rb. sphaeroides strain 2.4.1. The investigation reveals the structure of the carotenoid in the different protein preparations, the nature of its binding site, and a plausible mechanism by which the carotenoid is incorporated unidirectionally in its characteristic geometric configuration. The structural data suggest that the accessibility of the carotenoid to the binding site is controlled by a specific "gatekeeper" residue which allows the carotenoid to approach the binding site from only one direction. Carotenoid binding to the protein is secured by hydrogen bonding to a separate "locking" amino acid. The study reveals the specific molecular interactions that control how the carotenoid protects the photosynthetic apparatus against photo-induced oxidative destruction.
PubMed: 15130469
DOI: 10.1016/j.str.2004.02.037
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1rg5
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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