1E14

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M197 REPLACED WITH ARG (CHAIN M, FM197R) AND GLY M203 REPLACED WITH ASP (CHAIN M, GM203D)

1E14 の概要

• エントリーDOI: 10.2210/pdb1e14/pdb
• 関連するPDBエントリー: 1AIG 1AIJ 1MPS 1PCR 1PSS 1PST 1QOV 1YST 2RCR 4RCR
• 分子名称: Reaction center protein H chain, CARDIOLIPIN, Reaction center protein L chain, ... (11 entities in total)
• 機能のキーワード: transmembrane, electron transport, photosynthesis
• 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: 103833.53

構造登録者

Fyfe, P.K.,Ridge, J.P.,McAuley, K.E.,Cogdell, R.J.,Isaacs, N.W.,Jones, M.R. (登録日: 2000-04-18, 公開日: 2000-06-02, 最終更新日: 2024-05-01)

主引用文献

Fyfe, P.K.,Ridge, J.P.,Mcauley, K.E.,Cogdell, R.J.,Isaacs, N.W.,Jones, M.R.
Structural Consequences of the Replacement of Glycine M203 with Aspartic Acid in the Reaction Center from Rhodobacter Sphaeroides.
Biochemistry, 39:5953-, 2000

PubMed Abstract: Reaction centers with the double mutation Phe M197 to Arg and Gly M203 to Asp (FM197R/GM203D) have been crystallized from an antenna-deficient strain of Rhodobacter sphaeroides, and the structure has been determined at 2.7 A resolution. Unlike in reaction centers with a single FM197R mutation, the Arg M197 residue in the FM197R/GM203D reaction center adopts a position similar to that of the native Phe residue in the wild-type reaction center. Asp M203 is packed in such a way that the gamma-carboxy group interacts with the backbone carbonyl of Arg M197. The Asp M203 residue takes up part of the volume that is occupied in the wild-type reaction center by a water molecule. This water has been proposed to form a hydrogen bond interaction with the 9-keto carbonyl group of the active branch accessory bacteriochlorophyll, particularly when the primary donor bacteriochlorophylls are oxidized. The GM203D mutation therefore appears to remove the possibility of this hydrogen bond interaction by exclusion of this water molecule, as well as altering the local dielectric environment of the 9-keto carbonyl group. We examine whether the observed structural changes can provide new or alternative explanations for the absorbance and electron-transfer properties of reaction centers with the FM197R and GM203D mutations.

PubMed: 10821666
DOI: 10.1021/BI9925017

実験手法

X-RAY DIFFRACTION (2.7 Å)