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TitleCryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 5080, Year 2020
Publish dateOct 8, 2020
AuthorsSara J Weaver / Davi R Ortega / Matthew H Sazinsky / Triana N Dalia / Ankur B Dalia / Grant J Jensen /
PubMed AbstractNatural 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 ...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, binding to exogenous DNA, and retracting to thread this DNA through the outer membrane secretin, PilQ. Here, we use a functional tagged allele of VcPilQ purified from native V. cholerae cells to determine the cryoEM structure of the VcPilQ secretin in amphipol to ~2.7 Å. We use bioinformatics to examine the domain architecture and gene neighborhood of T4aP secretins in Proteobacteria in comparison with VcPilQ. This structure highlights differences in the architecture of the T4aP secretin from the type II and type III secretion system secretins. Based on our cryoEM structure, we design a series of mutants to reversibly regulate VcPilQ gate dynamics. These experiments support the idea of VcPilQ as a potential druggable target and provide insight into the channel that DNA likely traverses to promote the spread of antibiotic resistance via horizontal gene transfer by natural transformation.
External linksNat Commun / PubMed:33033258
MethodsEM (single particle)
Resolution2.7 Å
Structure data

EMDB-21559, PDB-6w6m:
Single particle cryoEM structure of V. cholerae Type IV competence pilus secretin PilQ
Method: EM (single particle) / Resolution: 2.7 Å

Source
  • vibrio cholerae (bacteria)
KeywordsTRANSPORT PROTEIN / secretion system / outer membrane protein

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