Evidence map›Paper›PMID 34402504›Full record

ArticleThe Biochemical journal2021

Cryo-EM structure of the Rhodospirillum rubrum RC-LH1 complex at 2.5 Å.

Pu Qian, Tristan I Croll, David J K Swainsbury, Pablo Castro-Hartmann, Nigel W Moriarty, Kasim Sader, C Neil Hunter

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

18 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. 2.4-Å structure of the double-ringScience advances · 2022
    Article
  16. Article
  17. Article
  18. 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

7 authors at 4 institutions in 6 countries.

Pu QianMaterials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, Netherlands.
Tristan I CrollCambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 0XY, U.K.
David J K SwainsburyDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, U.K.
Pablo Castro-HartmannMaterials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, Netherlands.
Nigel W MoriartyMolecular Biophysics and Integrated Bio-imaging, Lawrence Berkeley National Laboratory, Berkeley, CA 94720, U.S.A.
Kasim SaderMaterials and Structural Analysis, Thermo Fisher Scientific, Achtseweg Noord 5, 5651 GG Eindhoven, Netherlands.
C Neil HunterDepartment of Molecular Biology and Biotechnology, University of Sheffield, Sheffield, U.K.ORCID 0000-0003-2533-9783
Thermo Fisher Scientific (Netherlands) · NLUniversity of Sheffield · GBLawrence Berkeley National Laboratory · USUniversity of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M000265/1Wellcome Trust 209407/Z/17/Z
6 · The paper itself

Abstract

The reaction centre light-harvesting 1 (RC-LH1) complex is the core functional component of bacterial photosynthesis. We determined the cryo-electron microscopy (cryo-EM) structure of the RC-LH1 complex from Rhodospirillum rubrum at 2.5 Å resolution, which reveals a unique monomeric bacteriochlorophyll with a phospholipid ligand in the gap between the RC and LH1 complexes. The LH1 complex comprises a circular array of 16 αβ-polypeptide subunits that completely surrounds the RC, with a preferential binding site for a quinone, designated QP, on the inner face of the encircling LH1 complex. Quinols, initially generated at the RC QB site, are proposed to transiently occupy the QP site prior to traversing the LH1 barrier and diffusing to the cytochrome bc1 complex. Thus, the QP site, which is analogous to other such sites in recent cryo-EM structures of RC-LH1 complexes, likely reflects a general mechanism for exporting quinols from the RC-LH1 complex.

Indexed as

Bacterial ProteinsBacteriochlorophyllsBenzoquinonesBinding SitesCryoelectron MicroscopyCrystallizationElectron Transport Complex IIIHydrogen BondingHydroquinonesLigandsLight-Harvesting Protein ComplexesPhospholipidsProtein Conformation, alpha-HelicalRhodospirillum rubrumBacterial ProteinsBacteriochlorophyllsBenzoquinonesElectron Transport Complex IIIHydroquinonesLigandslight-harvesting complex 1, RhodospirillumLight-Harvesting Protein ComplexesPhospholipidsquinonecarotenoidscryo-electron microscopylight-harvestingphotosynthesisquinonereaction centre

Identifiers

PMID34402504
PMCPMC8454704
OpenAlexW3193345831

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.