Evidence map›Paper›PMID 29674684›Full record

ArticleNature communications2018

Cryo-EM structure of the RC-LH core complex from an early branching photosynthetic prokaryote.

Yueyong Xin, Yang Shi, Tongxin Niu, Qingqiang Wang, Wanqiang Niu, Xiaojun Huang, Wei Ding, Lei Yang, Robert E Blankenship, Xiaoling Xu and 1 more

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing 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

34 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Mining thermophile photosynthesis genes: a synthetic operon expressingbioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. A cytochrome cPlant communications · 2024
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 2.4-Å structure of the double-ringScience advances · 2022
    Article
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

11 authors.

Yueyong XinHangzhou Normal University, 2318 Yuhangtang Road, Cangqian, Yuhang District, Hangzhou, 311121, Zhejiang Province, China.ORCID http://orcid.org/0000-0002-0252-7346
Yang ShiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, 100101, Beijing, China.ORCID http://orcid.org/0000-0003-1579-7561
Tongxin NiuNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, 100101, Beijing, China.
Qingqiang WangHangzhou Normal University, 2318 Yuhangtang Road, Cangqian, Yuhang District, Hangzhou, 311121, Zhejiang Province, China.
Wanqiang NiuHangzhou Normal University, 2318 Yuhangtang Road, Cangqian, Yuhang District, Hangzhou, 311121, Zhejiang Province, China.
Xiaojun HuangCenter for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, 100101, Beijing, China.
Wei DingCenter for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, 100101, Beijing, China.
Lei YangHangzhou Normal University, 2318 Yuhangtang Road, Cangqian, Yuhang District, Hangzhou, 311121, Zhejiang Province, China.
Robert E BlankenshipDepartments of Biology and Chemistry, Washington University in St. Louis, St. Louis, MO, 63130, USA.ORCID http://orcid.org/0000-0003-0879-9489
Xiaoling XuHangzhou Normal University, 2318 Yuhangtang Road, Cangqian, Yuhang District, Hangzhou, 311121, Zhejiang Province, China. xuxl@hznu.edu.cn.ORCID http://orcid.org/0000-0001-8995-1213
Fei SunNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, 15 Datun Road, 100101, Beijing, China. feisun@ibp.ac.cn.ORCID http://orcid.org/0000-0002-0351-5144

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic prokaryotes evolved diverse light-harvesting (LH) antennas to absorb sunlight and transfer energy to reaction centers (RC). The filamentous anoxygenic phototrophs (FAPs) are important early branching photosynthetic bacteria in understanding the origin and evolution of photosynthesis. How their photosynthetic machinery assembles for efficient energy transfer is yet to be elucidated. Here, we report the 4.1 Å structure of photosynthetic core complex from Roseiflexus castenholzii by cryo-electron microscopy. The RC-LH complex has a tetra-heme cytochrome c bound RC encompassed by an elliptical LH ring that is assembled from 15 LHαβ subunits. An N-terminal transmembrane helix of cytochrome c inserts into the LH ring, not only yielding a tightly bound cytochrome c for rapid electron transfer, but also opening a slit in the LH ring, which is further flanked by a transmembrane helix from a newly discovered subunit X. These structural features suggest an unusual quinone exchange model of prokaryotic photosynthetic machinery.

Indexed as

Bacterial ProteinsChloroflexiCryoelectron MicroscopyCytochromes cHemeLightLight-Harvesting Protein ComplexesModels, MolecularPhotosynthetic Reaction Center Complex ProteinsBacterial ProteinsCytochromes cHemeLight-Harvesting Protein ComplexesPhotosynthetic Reaction Center Complex Proteins

Identifiers

PMID29674684
PMCPMC5908803

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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.