Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution



Bracun, Laura ORCID: 0000-0001-7698-3718, Yamagata, Atsushi, Christianson, Bern M, Terada, Tohru, Canniffe, Daniel P ORCID: 0000-0002-5022-0437, Shirouzu, Mikako and Liu, Lu-Ning ORCID: 0000-0002-8884-4819
(2021) Cryo-EM structure of the photosynthetic RC-LH1-PufX supercomplex at 2.8-Å resolution. SCIENCE ADVANCES, 7 (25). eabf8864-.

[img] Text
Final_2021_5_veldkampii RC-LH1_SA.pdf - Published version

Download (4MB) | Preview

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 <i>Rhodobacter veldkampii</i> 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.

Item Type: Article
Divisions: Faculty of Health and Life Sciences
Faculty of Health and Life Sciences > Institute of Systems, Molecular and Integrative Biology
Depositing User: Symplectic Admin
Date Deposited: 24 Jun 2021 07:48
Last Modified: 01 Feb 2024 08:49
DOI: 10.1126/sciadv.abf8864
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3127520