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Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels

DOI: 10.1126/sciadv.abe2631 DOI Help

Authors: David J. K. Swainsbury (University of Sheffield) , Pu Qian (University of Sheffield; Thermo Fisher Scientific) , Philip J. Jackson (University of Sheffield) , Kaitlyn M. Faries (Washington University in St. Louis) , Dariusz M. Niedzwiedzki (Washington University in St. Louis) , Elizabeth C. Martin (University of Sheffield) , David A. Farmer (Diamond Light Source) , Lorna A. Malone (University of Sheffield) , Rebecca F. Thompson (University of Leeds) , Neil A. Ranson (University of Leeds) , Daniel P. Canniffe (University of Liverpool) , Mark J. Dickman (University of Sheffield) , Dewey Holten (Washington University in St. Louis) , Christine Kirmaier (Washington University in St. Louis) , Andrew Hitchcock (University of Sheffield) , C. Neil Hunter (University of Sheffield)
Co-authored by industrial partner: Yes

Type: Journal Paper
Journal: Science Advances , VOL 7

State: Published (Approved)
Published: January 2021
Diamond Proposal Number(s): 19832

Open Access Open Access

Abstract: The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo–electron microscopy structures of RC-LH1 complexes from Rhodopseudomonas palustris. A 2.65-Å resolution structure of the RC-LH114-W complex consists of an open 14-subunit LH1 ring surrounding the RC interrupted by protein-W, whereas the complex without protein-W at 2.80-Å resolution comprises an RC completely encircled by a closed, 16-subunit LH1 ring. Comparison of these structures provides insights into quinone dynamics within RC-LH1 complexes, including a previously unidentified conformational change upon quinone binding at the RC QB site, and the locations of accessory quinone binding sites that aid their delivery to the RC. The structurally unique protein-W prevents LH1 ring closure, creating a channel for accelerated quinone/quinol exchange.

Diamond Keywords: Bacteria; Photosynthesis

Subject Areas: Biology and Bio-materials

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios II-Titan Krios II at Diamond

Documents:
eabe2631.full.pdf

Discipline Tags:

Organic Chemistry Life Sciences & Biotech Structural biology Chemistry Biochemistry

Technical Tags:

Microscopy Electron Microscopy (EM) Transmission Electron Microscopy (TEM)