Evidence map›Paper›PMID 17525736›Full record

ArticleThe EMBO journal2007

Preprotein-controlled catalysis in the helicase motor of SecA.

Spyridoula Karamanou, Giorgos Gouridis, Efrosyni Papanikou, Giorgos Sianidis, Ioannis Gelis, Dimitra Keramisanou, Eleftheria Vrontou, Charalampos G Kalodimos, Anastassios Economou

Abstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed.

  1. Review
  2. Article
  3. The Multifunctional Preprotein Binding Domain of SecA.Chembiochem : a European journal of chemical biology · 2024
    Article
  4. Article
  5. Review
  6. The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021
    Review
  7. Cotranslational folding of alkaline phosphatase in the periplasm of Escherichia coli.Protein science : a publication of the Protein Society · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017
    Review
  14. Using NMR spectroscopy to elucidate the role of molecular motions in enzyme function.Progress in nuclear magnetic resonance spectroscopy · 2016
    Review
  15. Article
  16. SecA: a potential antimicrobial target.Future medicinal chemistry · 2015
    Review
  17. Review
  18. Review
  19. Article
  20. 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

9 authors.

Spyridoula KaramanouInstitute of Molecular Biology and Biotechnology, Foundation of Research and Technology-Hellas, Crete, Greece.
Giorgos Gouridis
Efrosyni Papanikou
Giorgos Sianidis
Ioannis Gelis
Dimitra Keramisanou
Eleftheria Vrontou
Charalampos G Kalodimos
Anastassios Economou

Funding

Structural basis for the assembly of the Sec translocase machineryR01GM073854 · NIGMS · UNIVERSITY OF MINNESOTA · PI KALODIMOS, CHARALAMPOS · 2007 to 2016
$3.1M
NIGMS NIH HHS GM 73854NIGMS NIH HHS R01 GM073854
6 · The paper itself

Abstract

The cornerstone of the functionality of almost all motor proteins is the regulation of their activity by binding interactions with their respective substrates. In most cases, the underlying mechanism of this regulation remains unknown. Here, we reveal a novel mechanism used by secretory preproteins to control the catalytic cycle of the helicase 'DEAD' motor of SecA, the preprotein translocase ATPase. The central feature of this mechanism is a highly conserved salt-bridge, Gate1, that controls the opening/closure of the nucleotide cleft. Gate1 regulates the propagation of binding signal generated at the Preprotein Binding Domain to the nucleotide cleft, thus allowing the physical coupling of preprotein binding and release to the ATPase cycle. This relay mechanism is at play only after SecA has been previously 'primed' by binding to SecYEG, the transmembrane protein-conducting channel. The Gate1-controlled relay mechanism is essential for protein translocase catalysis and may be common in helicase motors.

Indexed as

Adenosine TriphosphatasesBacterial ProteinsCatalysisEnzyme ActivationMembrane Transport ProteinsProtein FoldingSecA ProteinsSEC Translocation ChannelsTemperatureAdenosine TriphosphatasesBacterial ProteinsMembrane Transport ProteinsSecA ProteinsSEC Translocation Channels

Identifiers

PMID17525736
PMCPMC1894763

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.