Evidence map›Paper›PMID 20100826›Full record

ArticleThe Journal of biological chemistry2010

Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway.

Seiji Ishii, Takato Yano, Akio Ebihara, Akihiro Okamoto, Miho Manzoku, Hideyuki Hayashi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

34 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
  2. Characterization of a novel glycocin from a thermophile.bioRxiv : the preprint server for biology · 2025
    Article
  3. Article
  4. Characterization of S-glycosylated glycocins containing three disulfides.Journal of industrial microbiology & biotechnology · 2024
    Article
  5. Virtual Screening of Inhibitors ofACS medicinal chemistry letters · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.Protein science : a publication of the Protein Society · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Biosynthesis and secretion of the microbial sulfated peptide RaxX and binding to the rice XA21 immune receptor.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Investigations into PoyH, a promiscuous protease from polytheonamide biosynthesis.Journal of industrial microbiology & biotechnology · 2019
    Article
  16. Article
  17. Article
  18. ABC transporter content diversity inProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Review
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 4 institutions in 1 country.

Seiji IshiiDepartment of Biochemistry, Osaka Medical College, Takatsuki, Osaka 569-8686, Japan.
Takato Yano
Akio Ebihara
Akihiro Okamoto
Miho Manzoku
Hideyuki Hayashi
Osaka Medical and Pharmaceutical University · JPGifu University · JPShizuoka University · JPSPring-8 · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ComA of Streptococcus is a member of the bacteriocin-associated ATP-binding cassette transporter family and is postulated to be responsible for both the processing of the propeptide ComC and secretion of the mature quorum-sensing signal. The 150-amino acid peptidase domain (PEP) of ComA specifically recognizes an extended region of ComC that is 15 amino acids in length. It has been proposed that an amphipathic alpha-helix formed by the N-terminal leader region of ComC, as well as the Gly-Gly motif at the cleavage site, is critical for the PEP-ComC interaction. To elucidate the substrate recognition mechanism, we determined the three-dimensional crystal structure of Streptococcus mutans PEP and then constructed models for the PEP.ComC complexes. PEP had an overall structure similar to the papain-like cysteine proteases as has long been predicted. The active site was located at the bottom of a narrow cleft, which is suitable for binding the Gly-Gly motif. Together with the results from mutational experiments, a shallow hydrophobic concave surface of PEP was proposed as a site that accommodates the N-terminal helix of ComC. This dual mode of substrate recognition would provide the small PEP domain with an extremely high substrate specificity.

Indexed as

Quorum SensingSignal TransductionATP-Binding Cassette TransportersBacterial ProteinsCircular DichroismCrystallography, X-RayModels, MolecularMutagenesis, Site-DirectedMutationPeptide HydrolasesProtein ConformationProtein Structure, TertiaryStreptococcusSubstrate SpecificityATP-Binding Cassette TransportersBacterial Proteinscompetence factor, StreptococcusPeptide Hydrolases

Identifiers

PMID20100826
PMCPMC2856284
OpenAlexW2031516694

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.