Evidence map›Paper›PMID 26389738›Full record

ArticleNature structural & molecular biology2015

Structure and multistate function of the transmembrane electron transporter CcdA.

Jessica A Williamson, Seung-Hyun Cho, Jiqing Ye, Jean-Francois Collet, Jonathan R Beckwith, James J Chou

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

19 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Journal of bacteriology · 2025
    Review
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  5. Review
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  7. Article
  8. Stress control for a well-structured life.The Journal of biological chemistry · 2018
    Article
  9. Review
  10. Article
  11. Article
  12. Article
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  14. Review
  15. Review
  16. Article
  17. Article
  18. A functional NMR for membrane proteins: dynamics, ligand binding, and allosteric modulation.Protein science : a publication of the Protein Society · 2016
    Review
  19. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Jessica A WilliamsonDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.ORCID http://orcid.org/0000-0002-5530-8657
Seung-Hyun ChoWELBIO, Brussels, Belgium.
Jiqing YeDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.
Jean-Francois ColletWELBIO, Brussels, Belgium.
Jonathan R BeckwithDepartment of Microbiology and Immunobiology, Harvard Medical School, Boston, Massachusetts, USA.
James J ChouDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts, USA.
Harvard University · USde Duve Institute · BE

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2014
$11.5M
Microbial Diversity in Mechanisms of Disulfide Bond Formation and ReductionR01GM041883 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BOYD, DANA · 1989 to 2014
$7.8M
AvanceIII 700MHz NMR spectrometer with cryogenic probeS10RR029236 · NCRR · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2010
$1.6M
Structural details of CcdA, a membrane transporter of thiol-reducing potentialR01GM079388 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2007 to 2010
$1.4M
European Research Council 282335NCRR NIH HHS S10 RR029236NIBIB NIH HHS P41 EB-002026NIBIB NIH HHS P41 EB002026NIGMS NIH HHS GM041883NIGMS NIH HHS GM094608NIGMS NIH HHS R01 GM079388NIGMS NIH HHS U54 GM094608
6 · The paper itself

Abstract

The mechanism by which transmembrane reductases use a single pair of cysteine residues to relay electrons between protein substrates across biological membranes is a long-standing mystery in thiol-redox biochemistry. Here we show the NMR structure of a reduced-state mimic of archaeal CcdA, a protein that transfers electrons across the inner membrane, by using a redox-active NMR sample. The two cysteine positions in CcdA are separated by 20 Å. Whereas one is accessible to the cytoplasm, the other resides in the protein core, thus implying that conformational exchange is required for periplasmic accessibility. In vivo mixed disulfide-trapping experiments validated the functional positioning of the cysteines, and in vitro accessibility results confirmed conformational exchange. Our NMR and functional data together show the existence of multiple conformational states and suggest a four-state model for relaying electrons from cytosolic to periplasmic redox substrates.

Indexed as

Models, MolecularAmino Acid SequenceArchaeal ProteinsCarrier ProteinsComputational BiologyCysteineElectronsMembrane ProteinsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularOxidoreductasesPlasmidsProtein ConformationArchaeal ProteinsCarrier ProteinsCysteineMembrane ProteinsOxidoreductases

Identifiers

PMID26389738
PMCPMC7871232
OpenAlexW2199967493

What OpenQuestion holds

Textmetadata
LicenceTDM
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.