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Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII

Diatoms rely on fucoxanthin chlorophyll a/c-binding proteins (FCPs) for their great success in oceans, which have a great diversity in their pigment, protein compositions, and subunit organizations. We report a unique structure of photosystem II (PSII)–FCPII supercomplex from Thalassiosira pseudonan...

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Autores principales: Feng, Yue, Li, Zhenhua, Li, Xiaoyi, Shen, Lili, Liu, Xueyang, Zhou, Cuicui, Zhang, Jinyang, Sang, Min, Han, Guangye, Yang, Wenqiang, Kuang, Tingyun, Wang, Wenda, Shen, Jian-Ren
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Association for the Advancement of Science 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10599620/
https://www.ncbi.nlm.nih.gov/pubmed/37878698
http://dx.doi.org/10.1126/sciadv.adi8446
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author Feng, Yue
Li, Zhenhua
Li, Xiaoyi
Shen, Lili
Liu, Xueyang
Zhou, Cuicui
Zhang, Jinyang
Sang, Min
Han, Guangye
Yang, Wenqiang
Kuang, Tingyun
Wang, Wenda
Shen, Jian-Ren
author_facet Feng, Yue
Li, Zhenhua
Li, Xiaoyi
Shen, Lili
Liu, Xueyang
Zhou, Cuicui
Zhang, Jinyang
Sang, Min
Han, Guangye
Yang, Wenqiang
Kuang, Tingyun
Wang, Wenda
Shen, Jian-Ren
author_sort Feng, Yue
collection PubMed
description Diatoms rely on fucoxanthin chlorophyll a/c-binding proteins (FCPs) for their great success in oceans, which have a great diversity in their pigment, protein compositions, and subunit organizations. We report a unique structure of photosystem II (PSII)–FCPII supercomplex from Thalassiosira pseudonana at 2.68-Å resolution by cryo–electron microscopy. FCPIIs within this PSII-FCPII supercomplex exist in dimers and monomers, and a homodimer and a heterodimer were found to bind to a PSII core. The FCPII homodimer is formed by Lhcf7 and associates with PSII through an Lhcx family antenna Lhcx6_1, whereas the heterodimer is formed by Lhcf6 and Lhcf11 and connects to the core together with an Lhcf5 monomer through Lhca2 monomer. An extended pigment network consisting of diatoxanthins, diadinoxanthins, fucoxanthins, and chlorophylls a/c is revealed, which functions in efficient light harvesting, energy transfer, and dissipation. These results provide a structural basis for revealing the energy transfer and dissipation mechanisms and also for the structural diversity of FCP antennas in diatoms.
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spelling pubmed-105996202023-10-26 Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII Feng, Yue Li, Zhenhua Li, Xiaoyi Shen, Lili Liu, Xueyang Zhou, Cuicui Zhang, Jinyang Sang, Min Han, Guangye Yang, Wenqiang Kuang, Tingyun Wang, Wenda Shen, Jian-Ren Sci Adv Biomedicine and Life Sciences Diatoms rely on fucoxanthin chlorophyll a/c-binding proteins (FCPs) for their great success in oceans, which have a great diversity in their pigment, protein compositions, and subunit organizations. We report a unique structure of photosystem II (PSII)–FCPII supercomplex from Thalassiosira pseudonana at 2.68-Å resolution by cryo–electron microscopy. FCPIIs within this PSII-FCPII supercomplex exist in dimers and monomers, and a homodimer and a heterodimer were found to bind to a PSII core. The FCPII homodimer is formed by Lhcf7 and associates with PSII through an Lhcx family antenna Lhcx6_1, whereas the heterodimer is formed by Lhcf6 and Lhcf11 and connects to the core together with an Lhcf5 monomer through Lhca2 monomer. An extended pigment network consisting of diatoxanthins, diadinoxanthins, fucoxanthins, and chlorophylls a/c is revealed, which functions in efficient light harvesting, energy transfer, and dissipation. These results provide a structural basis for revealing the energy transfer and dissipation mechanisms and also for the structural diversity of FCP antennas in diatoms. American Association for the Advancement of Science 2023-10-25 /pmc/articles/PMC10599620/ /pubmed/37878698 http://dx.doi.org/10.1126/sciadv.adi8446 Text en Copyright © 2023 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/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 Biomedicine and Life Sciences
Feng, Yue
Li, Zhenhua
Li, Xiaoyi
Shen, Lili
Liu, Xueyang
Zhou, Cuicui
Zhang, Jinyang
Sang, Min
Han, Guangye
Yang, Wenqiang
Kuang, Tingyun
Wang, Wenda
Shen, Jian-Ren
Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII
title Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII
title_full Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII
title_fullStr Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII
title_full_unstemmed Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII
title_short Structure of a diatom photosystem II supercomplex containing a member of Lhcx family and dimeric FCPII
title_sort structure of a diatom photosystem ii supercomplex containing a member of lhcx family and dimeric fcpii
topic Biomedicine and Life Sciences
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10599620/
https://www.ncbi.nlm.nih.gov/pubmed/37878698
http://dx.doi.org/10.1126/sciadv.adi8446
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