Evidence map›Paper›PMID 24443566›Full record

ArticleThe Journal of biological chemistry2014

Cryo-electron microscopic structure of SecA protein bound to the 70S ribosome.

Rajkumar Singh, Christian Kraft, Rahul Jaiswal, Kushal Sejwal, Vikram Babu Kasaragod, Jochen Kuper, Jörg Bürger, Thorsten Mielke, Joen Luirink, Shashi Bhushan

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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
  5. Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020
    Article
  6. Article
  7. Article
  8. Article
  9. Timing and specificity of cotranslational nascent protein modification in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  10. Article
  11. Article
  12. Review
  13. Direct visualization of theScience advances · 2019
    Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Recombinant Protein Expression System inFrontiers in microbiology · 2018
    Review
  19. Article
  20. SecA-a New Twist in the Tale.Journal of bacteriology · 2017
    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

10 authors at 4 institutions in 3 countries.

Rajkumar SinghRudolf Virchow Center/DFG Research Center for Experimental Biomedicine, University of Würzburg, Josef Schneider Str. 2, 97078 Würzburg, Germany.
Christian KraftRudolf Virchow Center/DFG Research Center for Experimental Biomedicine, University of Würzburg, Josef Schneider Str. 2, 97078 Würzburg, Germany.
Rahul JaiswalDivision of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, Singapore 637551.
Kushal SejwalRudolf Virchow Center/DFG Research Center for Experimental Biomedicine, University of Würzburg, Josef Schneider Str. 2, 97078 Würzburg, Germany.
Vikram Babu KasaragodRudolf Virchow Center/DFG Research Center for Experimental Biomedicine, University of Würzburg, Josef Schneider Str. 2, 97078 Würzburg, Germany.
Jochen KuperRudolf Virchow Center/DFG Research Center for Experimental Biomedicine, University of Würzburg, Josef Schneider Str. 2, 97078 Würzburg, Germany.
Jörg BürgerUltraStrukturNetzwerk, Max Planck Institute for Molecular Genetics, Ihnestr. 73, 14195 Berlin, Germany; Institut für Medizinische Physik und Biophysik, Charité, Ziegelstrasse 5-8, 10117 Berlin, Germany.
Thorsten MielkeUltraStrukturNetzwerk, Max Planck Institute for Molecular Genetics, Ihnestr. 73, 14195 Berlin, Germany; Institut für Medizinische Physik und Biophysik, Charité, Ziegelstrasse 5-8, 10117 Berlin, Germany.
Joen LuirinkDepartment of Molecular Microbiology, Institute of Molecular Cell Biology, Vrije Universiteit, 1081 HV Amsterdam, The Netherlands.
Shashi BhushanRudolf Virchow Center/DFG Research Center for Experimental Biomedicine, University of Würzburg, Josef Schneider Str. 2, 97078 Würzburg, Germany; Division of Structural Biology and Biochemistry, School of Biological Sciences, Nanyang Technological University, Singapore 637551. Electronic address: sbhushan@ntu.edu.sg.
University of Würzburg · DECharité - Universitätsmedizin Berlin · DENanyang Technological University · SGVrije Universiteit Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SecA is an ATP-dependent molecular motor pumping secretory and outer membrane proteins across the cytoplasmic membrane in bacteria. SecA associates with the protein-conducting channel, the heterotrimeric SecYEG complex, in a so-called posttranslational manner. A recent study further showed binding of a monomeric state of SecA to the ribosome. However, the true oligomeric state of SecA remains controversial because SecA can also form functional dimers, and high-resolution crystal structures exist for both the monomer and the dimer. Here we present the cryo-electron microscopy structures of Escherichia coli SecA bound to the ribosome. We show that not only a monomeric SecA binds to the ribosome but also that two copies of SecA can be observed that form an elongated dimer. Two copies of SecA completely surround the tunnel exit, providing a unique environment to the nascent polypeptides emerging from the ribosome. We identified the N-terminal helix of SecA required for a stable association with the ribosome. The structures indicate a possible function of the dimeric form of SecA at the ribosome.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsComputer SimulationCryoelectron MicroscopyEscherichia coli ProteinsMembrane Transport ProteinsModels, MolecularProtein BindingProtein Structure, SecondaryRibosome Subunits, Large, BacterialSecA ProteinsSEC Translocation ChannelsAdenosine TriphosphatasesBacterial ProteinsEscherichia coli ProteinsMembrane Transport ProteinsSecA ProteinsSEC Translocation Channels70SCryo-EMElectron Microscopy (EM)Protein SecretionProtein TranslocationRibosomeRibosomesSecASecYEGSingle Particle Analysis

Identifiers

PMID24443566
PMCPMC3945378
OpenAlexW2017580000

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.