The α-barrel tip region of Escherichia coli TolC homologs of Vibrio vulnificus interacts with the MacA protein to form the functional macrolide-specific efflux pump MacAB-TolC
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Title
The α-barrel tip region of Escherichia coli TolC homologs of Vibrio vulnificus interacts with the MacA protein to form the functional macrolide-specific efflux pump MacAB-TolC
Authors
Keywords
MacA, MacB, TolC, TolCV1, TolCV2, Type I secretion system
Journal
JOURNAL OF MICROBIOLOGY
Volume 51, Issue 2, Pages 154-159
Publisher
Springer Nature
Online
2013-05-01
DOI
10.1007/s12275-013-2699-3
References
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Note: Only part of the references are listed.- Assembly and Channel Opening of Outer Membrane Protein in Tripartite Drug Efflux Pumps of Gram-negative Bacteria
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- The assembled structure of a complete tripartite bacterial multidrug efflux pump
- (2009) M. F. Symmons et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Crystallization and preliminary X-ray crystallographic analysis of MacA fromActinobacillus actinomycetemcomitans
- (2008) Shunfu Piao et al. Acta Crystallographica Section F-Structural Biology and Crystallization Communications
- Structural and functional diversity of bacterial membrane fusion proteins
- (2008) Helen I. Zgurskaya et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- MacB ABC Transporter Is a Dimer Whose ATPase Activity and Macrolide-binding Capacity Are Regulated by the Membrane Fusion Protein MacA
- (2008) Hong Ting Lin et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Assembly and Channel Opening in a Bacterial Drug Efflux Machine
- (2008) Vassiliy N. Bavro et al. MOLECULAR CELL
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