2JBL

PHOTOSYNTHETIC REACTION CENTER FROM BLASTOCHLORIS VIRIDIS

「4PRC」から置き換えられました

2JBL の概要

• エントリーDOI: 10.2210/pdb2jbl/pdb
• 関連するPDBエントリー: 1DXR 1PRC 1R2C 1VRN 2PRC 3PRC 5PRC 6PRC 7PRC
• 分子名称: PHOTOSYNTHETIC REACTION CENTER CYTOCHROME C SUBUNIT, STIGMATELLIN A, FE (III) ION, ... (14 entities in total)
• 機能のキーワード: chromophore, formylation, chlorophyll, lipoprotein, stigmatellin, metal-binding, transmembrane, iron, heme, membrane, transport, magnesium, photosynthesis, reaction center, electron transport, bacteriochlorophyll, photosynthetic reaction center
• 由来する生物種: BLASTOCHLORIS VIRIDIS (RHODOPSEUDOMONAS VIRIDIS); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 145785.34

構造登録者

Lancaster, C.R.D. (登録日: 2006-12-08, 公開日: 2007-03-13, 最終更新日: 2024-11-20)

主引用文献

Lancaster, C.R.D.,Hunte, C.,Kelley, J.,Trumpower, B.L.,Ditchfield, R.
A Comparison of Stigmatellin Conformations, Free and Bound to the Photosynthetic Reaction Center and the Cytochrome Bc(1) Complex.
J.Mol.Biol., 368:197-, 2007

PubMed Abstract: We describe in detail the conformations of the inhibitor stigmatellin in its free form and bound to the ubiquinone-reducing (Q(B)) site of the reaction center and to the ubiquinol-oxidizing (Q(o)) site of the cytochrome bc(1) complex. We present here the first structures of a stereochemically correct stigmatellin in complexes with a bacterial reaction center and the yeast cytochrome bc1 complex. The conformations of the inhibitor bound to the two enzymes are not the same. We focus on the orientations of the stigmatellin side-chain relative to the chromone head group, and on the interaction of the stigmatellin side-chain with these membrane protein complexes. The different conformations of stigmatellin found illustrate the structural variability of the Q sites, which are affected by the same inhibitor. The free rotation about the chi1 dihedral angle is an essential factor for allowing stigmatellin to bind in both the reaction center and the cytochrome bc1 pocket.

PubMed: 17337272
DOI: 10.1016/J.JMB.2007.02.013

実験手法

X-RAY DIFFRACTION (2.4 Å)