Evidence map›Paper›PMID 32424145›Full record

ArticleNature communications2020

Structural basis for assembly and function of a diatom photosystem I-light-harvesting supercomplex.

Ryo Nagao, Koji Kato, Kentaro Ifuku, Takehiro Suzuki, Minoru Kumazawa, Ikuo Uchiyama, Yasuhiro Kashino, Naoshi Dohmae, Seiji Akimoto, Jian-Ren Shen and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.3field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

44 citing papers in PubMed, 102 citations in OpenAlex.

  1. Spectroscopic Investigation of the In Vivo Light-Dependent Photodynamics of the Marine Diatom Phaeodactylum tricornutum.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026
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  12. Structural insights into the assembly and energy transfer of haptophyte photosystem I-light-harvesting supercomplex.Proceedings of the National Academy of Sciences of the United States of America · 2024
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 7 institutions in 1 country.

Ryo Nagao *Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.
Koji Kato *Research Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.
Kentaro IfukuGraduate School of Biostudies, Kyoto University, Kyoto, 606-8502, Japan.ORCID http://orcid.org/0000-0003-0241-8008
Takehiro SuzukiBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, 351-0198, Japan.
Minoru KumazawaFaculty of Agriculture, Kyoto University, Kyoto, 606-8502, Japan.
Ikuo UchiyamaNational Institute for Basic Biology, National Institutes of Natural Sciences, Aichi, 444-8585, Japan.
Yasuhiro KashinoGraduate School of Life Science, University of Hyogo, Hyogo, 678-1297, Japan.ORCID http://orcid.org/0000-0002-4278-9359
Naoshi DohmaeBiomolecular Characterization Unit, RIKEN Center for Sustainable Resource Science, Saitama, 351-0198, Japan.
Seiji AkimotoGraduate School of Science, Kobe University, Hyogo, 657-8501, Japan.ORCID http://orcid.org/0000-0002-8951-8978
Jian-Ren ShenResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan.ORCID http://orcid.org/0000-0003-4471-8797
Naoyuki MiyazakiInstitute for Protein Research, Osaka University, Osaka, 565-0871, Japan. naomiyazaki@tara.tsukuba.ac.jp.ORCID http://orcid.org/0000-0002-4880-7300
Fusamichi AkitaResearch Institute for Interdisciplinary Science and Graduate School of Natural Science and Technology, Okayama University, Okayama, 700-8530, Japan. fusamichi_a@okayama-u.ac.jp.ORCID http://orcid.org/0000-0003-0537-6157
Okayama University of Science · JPKyoto University · JPRIKEN Center for Sustainable Resource Science · JPKobe University · JPNational Institute for Basic Biology · JPUniversity of Hyogo · JPUniversity of Tsukuba · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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-Å 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.

Indexed as

ChlorophyllChlorophyll Binding ProteinsDiatomsEnergy TransferLight-Harvesting Protein ComplexesModels, MolecularPhotosystem I Protein ComplexProtein BindingProtein SubunitsStructure-Activity RelationshipChlorophyllChlorophyll Binding ProteinsLight-Harvesting Protein ComplexesPhotosystem I Protein ComplexProtein Subunits

Identifiers

PMID32424145
PMCPMC7235021
OpenAlexW3024362141

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.