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-.
ISSN 2375-2548, 2375-2548
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Text
Swainsbury et al, 2021 Rps palustris RC-LH1 Structures.pdf - Published version Download (2MB) | Preview |
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 |
|---|---|
| Uncontrolled Keywords: | 34 Chemical Sciences, 3406 Physical Chemistry, 1.1 Normal biological development and functioning, Generic health relevance |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 14 Jan 2021 10:23 |
| Last Modified: | 07 Dec 2024 10:36 |
| DOI: | 10.1126/sciadv.abe2631 |
| Open Access URL: | https://advances.sciencemag.org/content/7/3/eabe26... |
| Related URLs: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3113607 |
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