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...
Autores principales: | , , , , , , , , , , , , , , , |
---|---|
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 |