JB
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Collins, R. F.
Right arrow Articles by Tønjum, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Collins, R. F.
Right arrow Articles by Tønjum, T.

Journal of Bacteriology, July 2001, p. 3825-3832, Vol. 183, No. 13
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.13.3825-3832.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Analysis of the PilQ Secretin from Neisseria meningitidis by Transmission Electron Microscopy Reveals a Dodecameric Quaternary Structure

Richard F. Collins,1 Linn Davidsen,2 Jeremy P. Derrick,1,* Robert C. Ford,1 and Tone Tønjum2

Department of Biomolecular Sciences, UMIST, Manchester, M60 1QD, United Kingdom,1 and Institute of Microbiology, Section of Molecular Microbiology, National Hospital, University of Oslo, N-0027 Oslo, Norway2

Received 1 February 2001/Accepted 10 April 2001

PilQ is a member of the secretin family of outer membrane proteins and is specifically involved in secretion of type IV pili in Neisseria meningitidis, Neisseria gonorrhoeae, and Pseudomonas aeruginosa. The quaternary structure of PilQ from N. meningitidis was analyzed by transmission electron microscopy by using a negative stain. Single particle averaging was carried out with a total data set of 650 individual particles, which produced a projection map generated from 296 particles at an estimated resolution of 2.6 nm. Oligomeric PilQ adopts a donut-like structure with an external ring that is 16.5 nm in diameter surrounding a central cavity that is 6.5 nm in diameter. Self-rotation and power spectrum analysis demonstrated the presence of 12-fold rotational symmetry, showing that PilQ is organized as a ring of 12 identical subunits. A model of the type IV meningococcal pilus fiber, based on the X-ray crystal structure of the N. gonorrhoeae pilin subunit, fitted neatly into the cavity, demonstrating how PilQ could serve as a channel for the growing pilus fiber.


* Corresponding author. Mailing address: Department of Biomolecular Sciences, UMIST, P.O. Box 88, Manchester, M60 1QD, United Kingdom. Phone: 0044 0161 200 4207. Fax: 0044 0161 236 0409. E-mail: Jeremy.Derrick{at}umist.ac.uk.


Journal of Bacteriology, July 2001, p. 3825-3832, Vol. 183, No. 13
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.13.3825-3832.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. Microbiol. Mol. Biol. Rev.
ALL ASM JOURNALS

Copyright © 2001 by the American Society for Microbiology. All rights reserved.