Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

The Journal of biological chemistry - 2 Apr 2010

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

Abstract excerpt

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 specifica...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ATP-Binding Cassette Transporters
Share to Circular Dichroism
Share to Crystallography, X-Ray

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutagenesis, Site-Directed

Share to Peptide Hydrolases

Share to Quorum Sensing

Share to Streptococcus

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 20100826
DOI: 10.1074/jbc.M109.093781
PMCID: PMC2856284

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20100826-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of the peptidase domain of Streptococcus ComA, a bifunctional ATP-binding cassette transporter involved in the quorum-sensing pathway.PMID 20100826Read ↗

Expression and characterization of the peptidase domain of Streptococcus pneumoniae ComA, a bifunctional ATP-binding cassette transporter involved in quorum sensing pathway.Semantic proximity Read ↗

High-throughput Screening of Small Molecule Inhibitors of the Streptococcus Quorum-sensing Signal PathwaySemantic proximity Read ↗

Boundary of the nucleotide-binding domain of Streptococcus ComA based on functional and structural analysis.Semantic proximity Read ↗

SepM, a Streptococcal Protease Involved in Quorum Sensing, Displays Strict Substrate Specificity.Semantic proximity Read ↗

Structure–Activity Relationships of the Competence Stimulating Peptide in Streptococcus mutans Reveal Motifs Critical for Membrane Protease SepM Recognition and ComD Receptor ActivationSemantic proximity Read ↗

Mapping the Structural Determinants of Quorum Sensing Activity in Streptococcus sinensis Via Mutational Analysis of Its Competence Stimulating Peptide.Semantic proximity Read ↗

Molecular characterization of group A streptococcal (GAS) oligopeptide permease (opp) and its effect on cysteine protease production.Semantic proximity Read ↗

Developing multispecies quorum-sensing modulators based on the Streptococcus mitis competence-stimulating peptide.Semantic proximity Read ↗

Pheromone Recognition and Selectivity by ComR Proteins among Streptococcus SpeciesSemantic proximity Read ↗

Genetic transformation in Streptococcus pneumoniae: nucleotide sequence analysis shows comA, a gene required for competence induction, to be a member of the bacterial ATP-dependent transport protein familySemantic proximity Read ↗

Deciphering the Regulatory Role and Molecular Interactions That Drive the Competence Regulon Quorum Sensing Circuitry in Streptococcus constellatusSemantic proximity Read ↗

Purification and functional studies of a potent modified quorum-sensing peptide and a two-peptide bacteriocin in Streptococcus mutans.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.