Cryo-EM Structure of the Type IV Pilus Extension ATPase from Enteropathogenic Escherichia coli
Author:
Affiliation:
1. Department of Physiology and Biophysics, Virginia Commonwealth University, Richmond, Virginia, USA
2. Department of Internal Medicine, Virginia Commonwealth University, Richmond, Virginia, USA
Abstract
Funder
HHS | NIH | NIAID | Division of Microbiology and Infectious Diseases, National Institute of Allergy and Infectious Diseases
HHS | NIH | National Institute of Arthritis and Musculoskeletal and Skin Diseases
Virginia Commonwealth University
Publisher
American Society for Microbiology
Subject
Virology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/mbio.02270-22
Reference43 articles.
1. Landmark Discoveries and Recent Advances in Type IV Pilus Research
2. Diversification of the type IV filament superfamily into machines for adhesion, protein secretion, DNA uptake, and motility
3. Type IV pili: dynamics, biophysics and functional consequences
4. DsbA is required for stability of the type IV pilin of enteropathogenicEscherichia coli
5. PilB and PilT Are ATPases Acting Antagonistically in Type IV Pilus Function in Myxococcus xanthus
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