Evidence map›Paper›PMID 31290743›Full record

ArticleeLife2019

HDX-MS reveals nucleotide-dependent, anti-correlated opening and closure of SecA and SecY channels of the bacterial translocon.

Zainab Ahdash, Euan Pyle, William John Allen, Robin A Corey, Ian Collinson, Argyris Politis

Open access · goldAbstract read
In one paragraph

Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Focusing onAntibiotics (Basel, Switzerland) · 2023
    Article
  6. Review
  7. Article
  8. Article
  9. Refined measurement of SecA-driven protein secretion reveals that translocation is indirectly coupled to ATP turnover.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Review
  11. 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

6 authors at 3 institutions in 1 country.

Zainab Ahdash *Department of Chemistry, King's College London, London, United Kingdom.ORCID 0000-0002-4495-8689
Euan Pyle *Department of Chemistry, King's College London, London, United Kingdom.ORCID 0000-0002-4633-4917
William John AllenSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-9513-4786
Robin A CoreyDepartment of Biochemistry, University of Oxford, Oxford, United Kingdom.ORCID 0000-0003-1820-7993
Ian CollinsonSchool of Biochemistry, University of Bristol, Bristol, United Kingdom.ORCID 0000-0002-3931-0503
Argyris PolitisDepartment of Chemistry, King's College London, London, United Kingdom.ORCID 0000-0002-6658-3224
King's College London · GBUniversity of Bristol · GBUniversity of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/I008675/1Biotechnology and Biological Sciences Research Council BB/M003604/1Biotechnology and Biological Sciences Research Council BB/N015126/1Medical Research Council MC_PC_15031Wellcome 109854/Z/15/Z
6 · The paper itself

Abstract

The bacterial Sec translocon is a multi-protein complex responsible for translocating diverse proteins across the plasma membrane. For post-translational protein translocation, the Sec-channel - SecYEG - associates with the motor protein SecA to mediate the ATP-dependent transport of pre-proteins across the membrane. Previously, a diffusional-based Brownian ratchet mechanism for protein secretion has been proposed; the structural dynamics required to facilitate this mechanism remain unknown. Here, we employ hydrogen-deuterium exchange mass spectrometry (HDX-MS) to reveal striking nucleotide-dependent conformational changes in the Sec protein-channel from

Indexed as

Hydrogen Deuterium Exchange-Mass SpectrometryAdenosine TriphosphateEscherichia coliEscherichia coli ProteinsIon Channel GatingNucleotidesProtein ConformationSecA ProteinsSEC Translocation ChannelsAdenosine TriphosphateEscherichia coli ProteinsNucleotidesSecA protein, E coliSecA ProteinsSEC Translocation ChannelsSecY protein, E coliconformational dynamicsE. colihydrogen-deuterium exchange mass spectromterymolecular biophysicsprotein translocationSecASecYEGstructural biology

Identifiers

PMID31290743
PMCPMC6639072
OpenAlexW2960040305

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.