Evidence map›Paper›PMID 35418573›Full record

ArticleNature communications2022

Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.

Peng Cao, Laura Bracun, Atsushi Yamagata, Bern M Christianson, Tatsuki Negami, Baohua Zou, Tohru Terada, Daniel P Canniffe, Mikako Shirouzu, Mei Li and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
4.8field-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

35 citing papers in PubMed, 56 citations in OpenAlex.

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  15. Tuning by Hydrogen Bonding in Photosynthesis.The journal of physical chemistry. B · 2024
    Article
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  19. Studies of the Functionalized α-Hydroxy-Molecules (Basel, Switzerland) · 2024
    Article
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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

11 authors at 4 institutions in 3 countries.

Peng Cao *National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Laura Bracun *Institute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.ORCID http://orcid.org/0000-0001-7698-3718
Atsushi Yamagata *Laboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan.ORCID http://orcid.org/0000-0001-9285-1256
Bern M ChristiansonInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Tatsuki NegamiDepartment of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.
Baohua ZouNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China.
Tohru TeradaDepartment of Biotechnology, Graduate School of Agricultural and Life Sciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo, 113-8657, Japan.ORCID http://orcid.org/0000-0002-7091-0646
Daniel P CanniffeInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK.
Mikako ShirouzuLaboratory for Protein Functional and Structural Biology, RIKEN Center for Biosystems Dynamics Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa, 230-0045, Japan. mikako.shirouzu@riken.jp.ORCID http://orcid.org/0000-0002-7997-2149
Mei LiNational Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China. meili@ibp.ac.cn.ORCID http://orcid.org/0000-0002-1742-2360
Lu-Ning LiuInstitute of Systems, Molecular and Integrative Biology, University of Liverpool, Liverpool, L69 7ZB, UK. luning.liu@liverpool.ac.uk.ORCID http://orcid.org/0000-0002-8884-4819
University of Liverpool · GBChinese Academy of Sciences · CNRIKEN Center for Biosystems Dynamics Research · JPThe University of Tokyo · JP

Funding

Biotechnology and Biological Sciences Research Council BB/R003890/1Biotechnology and Biological Sciences Research Council BB/V009729/1
6 · The paper itself

Abstract

The reaction center (RC) and light-harvesting complex 1 (LH1) form a RC-LH1 core supercomplex that is vital for the primary reactions of photosynthesis in purple phototrophic bacteria. Some species possess the dimeric RC-LH1 complex with a transmembrane polypeptide PufX, representing the largest photosynthetic complex in anoxygenic phototrophs. However, the details of the architecture and assembly mechanism of the RC-LH1 dimer are unclear. Here we report seven cryo-electron microscopy (cryo-EM) structures of RC-LH1 supercomplexes from Rhodobacter sphaeroides. Our structures reveal that two PufX polypeptides are positioned in the center of the S-shaped RC-LH1 dimer, interlocking association between the components and mediating RC-LH1 dimerization. Moreover, we identify another transmembrane peptide, designated PufY, which is located between the RC and LH1 subunits near the LH1 opening. PufY binds a quinone molecule and prevents LH1 subunits from completely encircling the RC, creating a channel for quinone/quinol exchange. Genetic mutagenesis, cryo-EM structures, and computational simulations provide a mechanistic understanding of the assembly and electron transport pathways of the RC-LH1 dimer and elucidate the roles of individual components in ensuring the structural and functional integrity of the photosynthetic supercomplex.

Indexed as

Photosynthetic Reaction Center Complex ProteinsRhodobacter sphaeroidesBacterial ProteinsBenzoquinonesCryoelectron MicroscopyLight-Harvesting Protein ComplexesModels, MolecularPeptidesPhotosynthesisBacterial ProteinsBenzoquinonesLight-Harvesting Protein ComplexesPeptidesPhotosynthetic Reaction Center Complex Proteinsquinone

Identifiers

PMID35418573
PMCPMC9007983
OpenAlexW4223475838

What OpenQuestion holds

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LicenceCC BY
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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.