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

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-LH1(14)-W complex consists of...

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Detalles Bibliográficos
Autores principales: 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, Hunter, C. Neil
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7806223/
https://www.ncbi.nlm.nih.gov/pubmed/33523887
http://dx.doi.org/10.1126/sciadv.abe2631
Descripción
Sumario: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-LH1(14)-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(B) 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.