Cargando…

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...

Descripción completa

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
_version_ 1783636482717646848
author 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
author_facet 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
author_sort Swainsbury, David J. K.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-7806223
institution National Center for Biotechnology Information
language English
publishDate 2021
publisher American Association for the Advancement of Science
record_format MEDLINE/PubMed
spelling pubmed-78062232021-01-21 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 Hunter, C. Neil Sci Adv Research Articles 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. American Association for the Advancement of Science 2021-01-13 /pmc/articles/PMC7806223/ /pubmed/33523887 http://dx.doi.org/10.1126/sciadv.abe2631 Text en Copyright © 2021 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY). https://creativecommons.org/licenses/by/4.0/ https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution license (https://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
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
Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels
title Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels
title_full Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels
title_fullStr Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels
title_full_unstemmed Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels
title_short Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels
title_sort structures of rhodopseudomonas palustris rc-lh1 complexes with open or closed quinone channels
topic Research Articles
url 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
work_keys_str_mv AT swainsburydavidjk structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT qianpu structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT jacksonphilipj structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT farieskaitlynm structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT niedzwiedzkidariuszm structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT martinelizabethc structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT farmerdavida structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT malonelornaa structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT thompsonrebeccaf structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT ransonneila structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT canniffedanielp structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT dickmanmarkj structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT holtendewey structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT kirmaierchristine structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT hitchcockandrew structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels
AT huntercneil structuresofrhodopseudomonaspalustrisrclh1complexeswithopenorclosedquinonechannels