Evidence map›Paper›PMID 22033919›Full record

ArticleThe Journal of biological chemistry2011

Conformational dynamics of the plug domain of the SecYEG protein-conducting channel.

Jelger A Lycklama A Nijeholt, Zht Cheng Wu, Arnold J M Driessen

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Functional asymmetry within the Sec61p translocon.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  10. The bacterial translocon SecYEG opens upon ribosome binding.The Journal of biological chemistry · 2013
    Article
  11. Article
  12. Direct simulation of early-stage Sec-facilitated protein translocation.Journal of the American Chemical Society · 2012
    Article
  13. The bacterial Sec-translocase: structure and mechanism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012
    Review
  14. 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

3 authors.

Jelger A Lycklama A NijeholtMolecular Microbiology, Groningen Biomolecular Sciences and Biotechnology institute, and the Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands.
Zht Cheng WuMolecular Microbiology, Groningen Biomolecular Sciences and Biotechnology institute, and the Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands.
Arnold J M DriessenMolecular Microbiology, Groningen Biomolecular Sciences and Biotechnology institute, and the Zernike Institute for Advanced Materials, University of Groningen, 9747 AG Groningen, The Netherlands. Electronic address: a.j.m.driessen@rug.nl.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The central pore of the SecYEG preprotein-conducting channel is closed at the periplasmic face of the membrane by a plug domain. To study its conformational dynamics, the plug was labeled site-specifically with an environment-sensitive fluorophore. In the presence of a stable preprotein translocation inter-mediate, the SecY plug showed an enhanced solvent exposure consistent with a displacement from the hydrophobic central pore region. In contrast, binding and insertion of a ribosome-bound nascent membrane protein did not alter the plug conformation. These data indicate different plug dynamics depending on the ligand bound state of the SecYEG channel.

Indexed as

Cell MembraneCrystallography, X-RayEscherichia coliEscherichia coli ProteinsFluorescent DyesHydrophobic and Hydrophilic InteractionsMethanococcusModels, MolecularMolecular ConformationPlasmidsProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProtein TransportRibosomesSEC Translocation ChannelsEscherichia coli ProteinsFluorescent DyesSEC Translocation Channels

Identifiers

PMID22033919
PMCPMC3243504

What OpenQuestion holds

Textmetadata
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.