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CryoEM Structure of the Vibrio cholerae Type IV Pilus Secretin PilQ

Weaver, Sara J. and Sazinsky, Matthew H. and Dalia, Triana N. and Dalia, Ankur B. and Jensen, Grant J. (2020) CryoEM Structure of the Vibrio cholerae Type IV Pilus Secretin PilQ. Biophysical Journal, 118 (3). 12a. ISSN 0006-3495. doi:10.1016/j.bpj.2019.11.247.

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Natural competence is the process by which bacteria take up genetic material from their environment and integrate it into their genome using homologous recombination. In Vibrio cholerae, the Type IV pilus (T4P) is thought to mediate DNA uptake by binding DNA and retracting back toward the cell. How the DNA enters the periplasm is unclear. One hypothesis suggests that the DNA-bound T4P retracts completely so that the DNA would pass through the outer membrane secretin pore (PilQ). PilQ is a 870 kDa outer membrane pore with C14 symmetry. Here, we purify the V. cholerae PilQ secretin from V. cholerae cells in amphipols for single particle cryogenic electron microscopy (cryoEM). We solve the structure to 3.5 Å and provide insight on the channel DNA may traverse through during uptake.

Item Type:Article
Related URLs:
URLURL TypeDescription ItemDiscussion Paper
Weaver, Sara J.0000-0001-7753-6215
Sazinsky, Matthew H.0000-0001-7550-5116
Dalia, Triana N.0000-0001-7614-1377
Dalia, Ankur B.0000-0003-2203-1230
Jensen, Grant J.0000-0003-1556-4864
Additional Information:© 2020 Biophysical Society. Available online 7 February 2020.
Issue or Number:3
Record Number:CaltechAUTHORS:20200210-091000513
Persistent URL:
Official Citation:Sara J. Weaver, Matthew Sazinsky, Triana Dalia, Ankur Dalia, Grant J. Jensen, CryoEM Structure of the Vibrio cholerae Type IV Pilus Secretin PilQ, Biophysical Journal, Volume 118, Issue 3, Supplement 1, 2020, Page 12a, ISSN 0006-3495, (
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:101192
Deposited By: Tony Diaz
Deposited On:10 Feb 2020 17:18
Last Modified:16 Nov 2021 18:00

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