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

Bracun, Laura, 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-.

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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
Uncontrolled Keywords:	1.1 Normal biological development and functioning, 1 Underpinning research
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:	15 Mar 2024 04:59
DOI:	10.1126/sciadv.abf8864
Related URLs:	Author Publisher
URI:	https://livrepository.liverpool.ac.uk/id/eprint/3127520