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

Research output: Journal article publicationJournal articleAcademic researchpeer-review

2 Citations (Scopus)


This study assessed the functional importance of residues located at the i-2position of face 4 of the tandem repeat loops of the quinolone resistance protein QnrVC7 through mutagenesis studies. The i-2position 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
Number of pages4
JournalAntimicrobial Agents and Chemotherapy
Issue number3
Publication statusPublished - 1 Mar 2016

ASJC Scopus subject areas

  • Pharmacology
  • Pharmacology (medical)
  • Infectious Diseases

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