Evidence map›Paper›PMID 39169020›Full record

ArticleNature communications2024

In situ structural determination of cyanobacterial phycobilisome-PSII supercomplex by STAgSPA strategy.

Xing Zhang, Yanan Xiao, Xin You, Shan Sun, Sen-Fang Sui

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Structural insight of a photosystem I-CpcL-phycobilisome supercomplex from a cyanobacteriumProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Cryo-EM single-particle analysis expanding towards increasingly native samples.Acta crystallographica. Section D, Structural biology · 2025
    Review
  10. Article
  11. Phycobilisome core architecture influences photoprotective quenching by the Orange Carotenoid Protein.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  12. Article
  13. Article
  14. The lumenal domain of Cyt bPhotosynthesis research · 2025
    Article
  15. Molecular glue for phycobilisome attachment to photosystem II inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Review
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

5 authors.

Xing Zhang *Ministry of Education Key Laboratory of Protein Sciences, Tsinghua-Peking Joint Center for Life Sciences, Beijing Frontier Research Center for Biological Structures, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China. zhxix@126.com.ORCID 0009-0005-4757-0224
Yanan Xiao *School of Life Sciences, Southern University of Science and Technology, Shenzhen, China.ORCID 0000-0001-9261-4947
Xin You *State Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structures, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.ORCID 0000-0002-9181-8646
Shan SunState Key Laboratory of Membrane Biology, Beijing Frontier Research Center for Biological Structures, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.ORCID 0000-0002-9807-626X
Sen-Fang SuiSchool of Life Sciences, Southern University of Science and Technology, Shenzhen, China. suisf@mail.tsinghua.edu.cn.ORCID 0000-0001-5253-2592

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32271245
6 · The paper itself

Abstract

Photosynthesis converting solar energy to chemical energy is one of the most important chemical reactions on earth. In cyanobacteria, light energy is captured by antenna system phycobilisomes (PBSs) and transferred to photosynthetic reaction centers of photosystem II (PSII) and photosystem I (PSI). While most of the protein complexes involved in photosynthesis have been characterized by in vitro structural analyses, how these protein complexes function together in vivo is not well understood. Here we implemented STAgSPA, an in situ structural analysis strategy, to solve the native structure of PBS-PSII supercomplex from the cyanobacteria Arthrospira sp. FACHB439 at resolution of ~3.5 Å. The structure reveals coupling details among adjacent PBSs and PSII dimers, and the collaborative energy transfer mechanism mediated by multiple super-PBS in cyanobacteria. Our results provide insights into the diversity of photosynthesis-related systems between prokaryotic cyanobacteria and eukaryotic red algae but are also a methodological demonstration for high-resolution structural analysis in cellular or tissue samples.

Indexed as

CyanobacteriaPhotosystem II Protein ComplexPhycobilisomesBacterial ProteinsCryoelectron MicroscopyEnergy TransferModels, MolecularPhotosynthesisPhotosystem I Protein ComplexBacterial ProteinsPhotosystem II Protein ComplexPhotosystem I Protein ComplexPhycobilisomes

Identifiers

PMID39169020
PMCPMC11339077

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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.