Site-Directed Mutagenesis Reveals Putative Substrate Binding Residues in the Escherichia coli RND Efflux Pump AcrB-Reference-Cited by-同舟云学术

Site-Directed Mutagenesis Reveals Putative Substrate Binding Residues in the Escherichia coli RND Efflux Pump AcrB

Published:2008-12-15 Issue:24 Volume:190 Page:8225-8229
ISSN:0021-9193
Container-title:Journal of Bacteriology
language:en
Short-container-title:J Bacteriol

Author:

Bohnert Jürgen A.¹,Schuster Sabine¹,Seeger Markus A.²,Fähnrich Eva¹,Pos Klaas M.²,Kern Winfried V.¹

Affiliation:

1. Center for Infectious Diseases and Travel Medicine, University Hospital, and Department of Medicine, Albert Ludwigs University, Freiburg, Germany

2. Institute of Physiology and Zürich Centre for Integrative Human Physiology, University of Zürich, Zürich, Switzerland

Abstract

ABSTRACT The Escherichia coli multidrug efflux pump protein AcrB has recently been cocrystallized with various substrates, suggesting that there is a phenylalanine-rich binding site around F178 and F615. We found that F610A was the point mutation that had the most significant impact on substrate MICs, while other targeted mutations, including conversion of phenylalanines 136, 178, 615, 617, and 628 to alanine, had smaller and more variable effects.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Link

https://journals.asm.org/doi/pdf/10.1128/JB.00912-08

Reference13 articles.

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3. Substrate Specificity of the RND-Type Multidrug Efflux Pumps AcrB and AcrD of Escherichia coli Is Determined Predominately by Two Large Periplasmic Loops

4. Mutations in the Central Cavity and Periplasmic Domain Affect Efflux Activity of the Resistance-Nodulation-Division Pump EmhB from Pseudomonas fluorescens cLP6a

5. Enhanced Expression of the Multidrug Efflux Pumps AcrAB and AcrEF Associated with Insertion Element Transposition in Escherichia coli Mutants Selected with a Fluoroquinolone

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