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

CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.

Nature communications - 8 Oct 2020

Weaver Sara J, Ortega Davi R, Sazinsky Matthew H, Dalia Triana N, Dalia Ankur B, Jensen Grant J

Abstract excerpt

Natural transformation is the process by which bacteria take up genetic material from their environment and integrate it into their genome by homologous recombination. It represents one mode of horizontal gene transfer and contributes to the spread of traits like antibiotic resistance. In Vibrio cholerae, a type IVa pilus (T4aP) is thought to facilitate natural transformation by extending from the cell surface,...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Secretion Systems
Share to Cryoelectron Microscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cysteine

Share to Fimbriae, Bacterial

Share to Models, Molecular

Share to Protein Domains

Share to Transformation, Bacterial

Share to Vibrio cholerae

Source

Open in PubMed Open full text

Identifiers

PMID: 33033258
DOI: 10.1038/s41467-020-18866-y
PMCID: PMC7545093

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.PMID 33033258Read ↗

Architecture of the Vibrio cholerae toxin-coregulated pilus machine revealed by electron cryotomography.Semantic proximity Read ↗

Cryo-EM structures of type IV pili complexed with nanobodies reveal immune escape mechanismsSemantic proximity Read ↗

A new twist on bacterial motility – two distinct type IV pili revealed by cryoEMSemantic proximity Read ↗

Topology of the outer-membrane secretin PilQ from Neisseria meningitidis.Semantic proximity Read ↗

<i>In situ</i> Architecture of the Tad Pilus Machine in <i>Caulobacter crescentus</i>Semantic proximity Read ↗

A broad-spectrum phage-encoded mechanism to disarm bacterial type IV filamentsSemantic proximity Read ↗

Architecture of the type IVa pilus machine.Semantic proximity Read ↗

PilF is an outer membrane lipoprotein required for multimerization and localization of the Pseudomonas aeruginosa Type IV pilus secretin.Semantic proximity Read ↗

Structure of the competence pilus major pilin ComGC in Streptococcus pneumoniaeSemantic proximity Read ↗

Structural determinants of endopilus assembly, stability and functional specificity in bacterial type II secretionSemantic proximity Read ↗

Cryo-EM analysis of Pseudomonas phage Pa193 structural componentsSemantic proximity Read ↗

Structure of CFA/I fimbriae from enterotoxigenic Escherichia coli.Semantic proximity Read ↗

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