Structures of <i>Rhodopseudomonas palustris</i> RC-LH1 complexes with open or closed quinone channels



Swainsbury, David JK, 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
et al (show 6 more authors) (2021) Structures of <i>Rhodopseudomonas palustris</i> RC-LH1 complexes with open or closed quinone channels. SCIENCE ADVANCES, 7 (3). eabe2631-.

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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 <i>Rhodopseudomonas palustris</i> A 2.65-Å resolution structure of the RC-LH1<sub>14</sub>-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 Q<sub>B</sub> 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
Depositing User: Symplectic Admin
Date Deposited: 14 Jan 2021 10:23
Last Modified: 09 Feb 2024 02:58
DOI: 10.1126/sciadv.abe2631
Open Access URL: https://advances.sciencemag.org/content/7/3/eabe26...
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URI: https://livrepository.liverpool.ac.uk/id/eprint/3113607