8YGL

Rhodobacter blasticus RC-LH1 monomer

8YGL の概要

• エントリーDOI: 10.2210/pdb8ygl/pdb
• EMDBエントリー: 39255
• 分子名称: Antenna pigment protein beta chain, CARDIOLIPIN, BACTERIOPHEOPHYTIN A, ... (13 entities in total)
• 機能のキーワード: photosynthesis, light-harvesting complex
• 由来する生物種: Fuscovulum blasticum DSM 2131; 詳細
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 361517.51

構造登録者

Liu, L.N.,Zhang, Y.Z.,Wang, P.,Christianson, B.M.,Ugurlar, D. (登録日: 2024-02-26, 公開日: 2025-03-05)

主引用文献

Wang, P.,Christianson, B.M.,Ugurlar, D.,Mao, R.,Zhang, Y.,Liu, Z.K.,Zhang, Y.Y.,Gardner, A.M.,Gao, J.,Zhang, Y.Z.,Liu, L.N.
Architectures of photosynthetic RC-LH1 supercomplexes from Rhodobacter blasticus.
Sci Adv, 10:eadp6678-eadp6678, 2024

PubMed Abstract: The reaction center-light-harvesting complex 1 (RC-LH1) plays an essential role in the primary reactions of bacterial photosynthesis. Here, we present high-resolution structures of native monomeric and dimeric RC-LH1 supercomplexes from () using cryo-electron microscopy. The RC-LH1 monomer is composed of an RC encircled by an open LH1 ring comprising 15 αβ heterodimers and a PufX transmembrane polypeptide. In the RC-LH1 dimer, two crossing PufX polypeptides mediate dimerization. Unlike counterpart, RC-LH1 dimer has a less bent conformation, lacks the PufY subunit near the LH1 opening, and includes two extra LH1 αβ subunits, forming a more enclosed S-shaped LH1 ring. Spectroscopic assays reveal that these unique structural features are accompanied by changes in the kinetics of quinone/quinol trafficking between RC-LH1 and cytochrome . Our findings reveal the assembly principles and structural variability of photosynthetic RC-LH1 supercomplexes, highlighting diverse strategies used by phototrophic bacteria to optimize light-harvesting and electron transfer in competitive environments.

PubMed: 39383221
DOI: 10.1126/sciadv.adp6678

実験手法

ELECTRON MICROSCOPY (2.6 Å)