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7YML

Structure of photosynthetic LH1-RC super-complex of Rhodobacter capsulatus

7YML の概要
エントリーDOI10.2210/pdb7yml/pdb
EMDBエントリー33931
分子名称Reaction center protein L chain, (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE, 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine, ... (17 entities in total)
機能のキーワードlh1-rc complex, photosynthesis, purple bacteria
由来する生物種Rhodobacter capsulatus
詳細
タンパク質・核酸の鎖数24
化学式量合計280968.64
構造登録者
主引用文献Tani, K.,Kanno, R.,Ji, X.C.,Satoh, I.,Kobayashi, Y.,Hall, M.,Yu, L.J.,Kimura, Y.,Mizoguchi, A.,Humbel, B.M.,Madigan, M.T.,Wang-Otomo, Z.Y.
Rhodobacter capsulatus forms a compact crescent-shaped LH1-RC photocomplex.
Nat Commun, 14:846-846, 2023
Cited by
PubMed Abstract: Rhodobacter (Rba.) capsulatus has been a favored model for studies of all aspects of bacterial photosynthesis. This purple phototroph contains PufX, a polypeptide crucial for dimerization of the light-harvesting 1-reaction center (LH1-RC) complex, but lacks protein-U, a U-shaped polypeptide in the LH1-RC of its close relative Rba. sphaeroides. Here we present a cryo-EM structure of the Rba. capsulatus LH1-RC purified by DEAE chromatography. The crescent-shaped LH1-RC exhibits a compact structure containing only 10 LH1 αβ-subunits. Four αβ-subunits corresponding to those adjacent to protein-U in Rba. sphaeroides were absent. PufX in Rba. capsulatus exhibits a unique conformation in its N-terminus that self-associates with amino acids in its own transmembrane domain and interacts with nearby polypeptides, preventing it from interacting with proteins in other complexes and forming dimeric structures. These features are discussed in relation to the minimal requirements for the formation of LH1-RC monomers and dimers, the spectroscopic behavior of both the LH1 and RC, and the bioenergetics of energy transfer from LH1 to the RC.
PubMed: 36792596
DOI: 10.1038/s41467-023-36460-w
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (2.6 Å)
構造検証レポート
Validation report summary of 7yml
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2026-02-04に公開中

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