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6W6M

Single particle cryoEM structure of V. cholerae Type IV competence pilus secretin PilQ

Summary for 6W6M
Entry DOI10.2210/pdb6w6m/pdb
EMDB information21559
DescriptorType IV pilus secretin PilQ family protein (1 entity in total)
Functional Keywordssecretion system, outer membrane protein, transport protein
Biological sourceVibrio cholerae
Total number of polymer chains14
Total formula weight874428.63
Authors
Sazinsky, M.H.,Weaver, S.J. (deposition date: 2020-03-17, release date: 2020-10-14, Last modification date: 2024-03-06)
Primary citationWeaver, S.J.,Ortega, D.R.,Sazinsky, M.H.,Dalia, T.N.,Dalia, A.B.,Jensen, G.J.
CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.
Nat Commun, 11:5080-5080, 2020
Cited by
PubMed Abstract: 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.
PubMed: 33033258
DOI: 10.1038/s41467-020-18866-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.7 Å)
Structure validation

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