1RGN

Structure of the reaction centre from Rhodobacter sphaeroides carotenoidless strain R-26.1 reconstituted with spheroidene

1RGN の概要

• エントリーDOI: 10.2210/pdb1rgn/pdb
• 関連するPDBエントリー: 1RG5 1RQK 4RCR
• 分子名称: Reaction center protein L chain, SPHEROIDENE, Reaction center protein M chain, ... (11 entities in total)
• 機能のキーワード: photosynthesis, photosynthetic reaction center, reconstituted carotenoid, 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: 103058.53

構造登録者

Roszak, A.W.,Frank, H.A.,McKendrick, K.,Mitchell, I.A.,Cogdell, R.J.,Isaacs, N.W. (登録日: 2003-11-12, 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

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

実験手法

X-RAY DIFFRACTION (2.8 Å)