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Mutational Analysis of Quinolone Resistance Protein QnrVC7 Provides Novel Insights into the Structure-Activity Relationship of Qnr Proteins

  • Kathy Hiu Laam Po
  • , Edward Wai Chi Chan
  • , Sheng Chen*
  • *Corresponding author for this work

Research output: Journal Publications and ReviewsRGC 21 - Publication in refereed journalpeer-review

Abstract

This study assessed the functional importance of residues located at the i-2 position of face 4 of the tandem repeat loops of the quinolone resistance protein QnrVC7 through mutagenesis studies. The i-2 position of face 4 on different coils required residues with different natures. Some substitutions reduced the protective activity of QnrVC7, while some of them increased it. These findings advanced our understanding on the detailed structural organization and functional requirements of Qnr proteins.
Original languageEnglish
Pages (from-to)1939-1942
JournalAntimicrobial Agents and Chemotherapy
Volume60
Issue number3
Online published26 Feb 2016
DOIs
Publication statusPublished - Mar 2016
Externally publishedYes

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