7DDQ

Structure of RC-LH1-PufX from Rhodobacter veldkampii

7DDQ の概要

• エントリーDOI: 10.2210/pdb7ddq/pdb
• EMDBエントリー: 30656
• 分子名称: Antenna pigment protein alpha chain, BACTERIOPHEOPHYTIN A, FE (III) ION, ... (12 entities in total)
• 機能のキーワード: membrane protein, light-harvesting, reaction center, pufx, photosynthesis
• 由来する生物種: Rhodobacter veldkampii DSM 11550; 詳細
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 335120.87

構造登録者

Bracun, L.,Yamagata, A.,Shirouzu, M.,Liu, L.N. (登録日: 2020-10-29, 公開日: 2021-06-30, 最終更新日: 2025-06-25)

主引用文献

Bracun, L.,Yamagata, A.,Christianson, B.M.,Terada, T.,Canniffe, D.P.,Shirouzu, M.,Liu, L.N.
Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-angstrom resolution.
Sci Adv, 7:-, 2021

PubMed Abstract: The reaction center (RC)-light-harvesting complex 1 (LH1) supercomplex plays a pivotal role in bacterial photosynthesis. Many RC-LH1 complexes integrate an additional protein PufX that is key for bacterial growth and photosynthetic competence. Here, we present a cryo-electron microscopy structure of the RC-LH1-PufX supercomplex from at 2.8-Å resolution. The RC-LH1-PufX monomer contains an LH ring of 15 αβ-polypeptides with a 30-Å gap formed by PufX. PufX acts as a molecular "cross brace" to reinforce the RC-LH1 structure. The unusual PufX-mediated large opening in the LH1 ring and defined arrangement of proteins and cofactors provide the molecular basis for the assembly of a robust RC-LH1-PufX supercomplex and efficient quinone transport and electron transfer. These architectural features represent the natural strategies for anoxygenic photosynthesis and environmental adaptation.

PubMed: 34134992
DOI: 10.1126/sciadv.abf8864

実験手法

ELECTRON MICROSCOPY (2.84 Å)