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

Swainsbury, David J. K., Qian, Pu, Jackson, Philip J., Faries, Kaitlyn M., Niedzwiedzki, Dariusz M., Martin, Elizabeth C., Farmer, David A., Malone, Lorna A., Thompson, Rebecca F., Ranson, Neil A., Canniffe, Daniel P., Dickman, Mark J., Holten, Dewey, Kirmaier, Christine, Hitchcock, Andrew and Hunter, C. Neil (2021) Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels. Science Advances, 7 (3). ISSN 2375-2548

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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.

Item Type: Article
Additional Information: Funding: D.J.K.S., P.Q., P.J.J., E.C.M., D.P.C., A.H., and C.N.H. were supported by the Biotechnology and Biological Sciences Research Council award number BB/M000265/1. A.H. also acknowledges support from a Royal Society University Research Fellowship (award number URF\R1\191548). C.N.H. further acknowledges Engineering and Physical Sciences Research Council award number EP/S002103/1 and European Research Council Synergy award number 854126. K.M.F., D.M.N., C.K., and D.H. acknowledge support by the Photosynthetic Antenna Research Center (PARC), an Energy Frontier Research Center funded by the U.S. Department of Energy, Office of Science, and Office of Basic Energy Sciences under Award Number DE-SC 0001035 for the photophysical studies. D.A.F. was supported by a University of Sheffield doctoral scholarship. L.A.M. was supported by a White Rose doctoral studentship. R.F.T. and N.A.R were funded by the University of Leeds (UoL ABSL award) and Wellcome Trust (108466/Z/15/Z). M.J.D. acknowledges support from the Biotechnology and Biological Sciences Research Council (United Kingdom) (BB/M012166/1).
Uncontrolled Keywords: general ,/dk/atira/pure/subjectarea/asjc/1000
Faculty \ School: Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 17 Aug 2022 14:30
Last Modified: 24 Sep 2022 07:03
URI: https://ueaeprints.uea.ac.uk/id/eprint/87388
DOI: 10.1126/sciadv.abe2631

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