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ID 59912
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Nagao, Ryo Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University Kaken ID publons researchmap
Kato, Koji Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID publons researchmap
Ifuku, Kentaro Graduate School of Biostudies, Kyoto University
Suzuki, Takehiro Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Kumazawa, Minoru Faculty of Agriculture, Kyoto University
Uchiyama, Ikuo National Institute for Basic Biology, National Institutes of Natural Sciences
Kashino, Yasuhiro Graduate School of Life Science, University of Hyogo
Dohmae, Naoshi Biomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science
Akimoto, Seiji Graduate School of Science,Kobe University
Shen, Jian-Ren Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID publons researchmap
Miyazaki, Naoyuki Institute for Protein Research, Osaka University
Akita, Fusamichi Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University ORCID Kaken ID publons researchmap
Abstract
Photosynthetic light-harvesting complexes (LHCs) play a pivotal role in collecting solar energy for photochemical reactions in photosynthesis. One of the major LHCs are fucoxanthin chlorophyll a/c-binding proteins (FCPs) present in diatoms, a group of organisms having important contribution to the global carbon cycle. Here, we report a 2.40-angstrom resolution structure of the diatom photosystem I (PSI)-FCPI supercomplex by cryo-electron microscopy. The supercomplex is composed of 16 different FCPI subunits surrounding a monomeric PSI core. Each FCPI subunit showed different protein structures with different pigment contents and binding sites, and they form a complicated pigment-protein network together with the PSI core to harvest and transfer the light energy efficiently. In addition, two unique, previously unidentified subunits were found in the PSI core. The structure provides numerous insights into not only the light-harvesting strategy in diatom PSI-FCPI but also evolutionary dynamics of light harvesters among oxyphototrophs. One of the major photosynthetic light-harvesting complexes (LHCs) are fucoxanthin chlorophyll a/c-binding proteins (FCPs), which are present in diatoms, a major group of algae. Here, the authors present the cryo-EM structure of the photosystem I-FCP (PSI-FCPI) supercomplex isolated from the marine centric diatom Chaetoceros gracilis that contains 16 FCPI subunits surrounding the PSI core and discuss possible excitation energy transfer pathways.
Published Date
2020-05-18
Publication Title
Nature Communications
Volume
volume11
Issue
issue1
Publisher
Nature Research
ISSN
2041-1723
Content Type
Journal Article
language
英語
OAI-PMH Set
岡山大学
Copyright Holders
© The Author(s) 2020
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publisher
PubMed ID
DOI
Web of Science KeyUT
Related Url
isVersionOf https://doi.org/10.1038/s41467-020-16324-3
License
http://creativecommons.org/licenses/by/4.0/
Funder Name
Japan Society for the Promotion of Science
助成番号
17K07442
19H04726
16H06553
17H06433