2WJM

Lipidic sponge phase crystal structure of the photosynthetic reaction centre from Blastochloris viridis (low dose)

2WJM の概要

• エントリーDOI: 10.2210/pdb2wjm/pdb
• 関連するPDBエントリー: 1DXR 1PRC 1R2C 1VRN 2JBL 2PRC 2WJN 3PRC 5PRC 6PRC 7PRC
• 分子名称: PHOTOSYNTHETIC REACTION CENTER CYTOCHROME C SUBUNIT, FE (II) ION, MENAQUINONE-7, ... (14 entities in total)
• 機能のキーワード: reaction centre, photosynthesis, membrane protein, lipids, monoolein, posttranslational modification, thioether bond, ubiquinone, lipidic sponge phase
• 由来する生物種: RHODOPSEUDOMONAS VIRIDIS; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 143688.63

構造登録者

Woehri, A.B.,Wahlgren, W.Y.,Malmerberg, E.,Johansson, L.C.,Neutze, R.,Katona, G. (登録日: 2009-05-27, 公開日: 2009-09-22, 最終更新日: 2024-11-06)

主引用文献

Wohri, A.B.,Wahlgren, W.Y.,Malmerberg, E.,Johansson, L.C.,Neutze, R.,Katona, G.
Lipidic sponge phase crystal structure of a photosynthetic reaction center reveals lipids on the protein surface.
Biochemistry, 48:9831-9838, 2009

PubMed Abstract: Membrane proteins are embedded in a lipid bilayer and maintain strong interactions with lipid molecules. Tightly bound lipids are responsible for vertical positioning and integration of proteins in the membrane and for assembly of multisubunit complexes and occasionally act as substrates. In this work we present the lipidic sponge phase crystal structure of the reaction center from Blastochloris viridis to 1.86 A, which reveals lipid molecules interacting with the protein surface. A diacylglycerol molecule is bound, through a thioether bond, to the N-terminus of the tetraheme cytochrome c subunit. From the electron density recovered at the Q(B) site and the observed change in recombination kinetics in lipidic sponge phase-grown crystals, the mobile ubiquinone appears to be displaced by a monoolein molecule. A 36 A long electron density feature is observed at the interface of transmembrane helices belonging to the H- and M-subunits, probably arising from an unidentified lipid.

PubMed: 19743880
DOI: 10.1021/bi900545e

実験手法

X-RAY DIFFRACTION (1.95 Å)