Evidence map›Paper›PMID 27534696›Full record

ArticleNature communications2016

In situ high-resolution structure of the baseplate antenna complex in Chlorobaculum tepidum.

Jakob Toudahl Nielsen, Natalia V Kulminskaya, Morten Bjerring, Juha M Linnanto, Margus Rätsep, Marie Østergaard Pedersen, Petar H Lambrev, Márta Dorogi, Győző Garab, Karen Thomsen and 4 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

10 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacteriumProceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  6. Editorial.Photosynthetica · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. 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

14 authors at 7 institutions in 4 countries.

Jakob Toudahl NielsenCenter for Insoluble Protein Structures (inSPIN), Aarhus C DK-8000, Denmark.
Natalia V KulminskayaCenter for Insoluble Protein Structures (inSPIN), Aarhus C DK-8000, Denmark.
Morten BjerringCenter for Insoluble Protein Structures (inSPIN), Aarhus C DK-8000, Denmark.
Juha M LinnantoInstitute of Physics, University of Tartu, W. Ostwaldi Street 1, Tartu 50411, Estonia.
Margus RätsepInstitute of Physics, University of Tartu, W. Ostwaldi Street 1, Tartu 50411, Estonia.
Marie Østergaard PedersenCenter for Insoluble Protein Structures (inSPIN), Aarhus C DK-8000, Denmark.
Petar H LambrevHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, Szeged 6726, Hungary.
Márta DorogiHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, Szeged 6726, Hungary.
Győző GarabHungarian Academy of Sciences, Biological Research Centre, Temesvári krt. 62, Szeged 6726, Hungary.
Karen ThomsenInterdisciplinary Nanoscience Center (iNANO), Aarhus University, Gustav Wieds Vej 14, Aarhus C DK-8000, Denmark.
Caroline JegerschöldKarolinska Institutet, Department of Biosciences and Medical Nutrition, Hälsovägen 7, Huddinge 141 83, Sweden.
Niels-Ulrik FrigaardSection for Marine Biology, Department of Biology, University of Copenhagen, Strandpromenaden 5, Helsingør DK-3000, Denmark.
Martin LindahlKarolinska Institutet, Department of Biosciences and Medical Nutrition, Hälsovägen 7, Huddinge 141 83, Sweden.
Niels Chr NielsenCenter for Insoluble Protein Structures (inSPIN), Aarhus C DK-8000, Denmark.
Aarhus University · DKHUN-REN Szegedi Biológiai Kutatóközpont · HUKarolinska Institutet · SEUniversity of Tartu · EEHungarian Academy of Sciences · HUNovo Nordisk (Denmark) · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Photosynthetic antenna systems enable organisms harvesting light and transfer the energy to the photosynthetic reaction centre, where the conversion to chemical energy takes place. One of the most complex antenna systems, the chlorosome, found in the photosynthetic green sulfur bacterium Chlorobaculum (Cba.) tepidum contains a baseplate, which is a scaffolding super-structure, formed by the protein CsmA and bacteriochlorophyll a. Here we present the first high-resolution structure of the CsmA baseplate using intact fully functional, light-harvesting organelles from Cba. tepidum, following a hybrid approach combining five complementary methods: solid-state NMR spectroscopy, cryo-electron microscopy, isotropic and anisotropic circular dichroism and linear dichroism. The structure calculation was facilitated through development of new software, GASyCS for efficient geometry optimization of highly symmetric oligomeric structures. We show that the baseplate is composed of rods of repeated dimers of the strongly amphipathic CsmA with pigments sandwiched within the dimer at the hydrophobic side of the helix.

Indexed as

AnisotropyChlorobiCircular DichroismCryoelectron MicroscopyImaging, Three-DimensionalLight-Harvesting Protein ComplexesMagnetic Resonance SpectroscopyModels, MolecularOrganellesReproducibility of ResultsLight-Harvesting Protein Complexes

Identifiers

PMID27534696
PMCPMC4992139
OpenAlexW2514538596

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.