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

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review

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Author(s)

Detail(s)

Original languageEnglish
Pages (from-to)1939-1942
Journal / PublicationAntimicrobial Agents and Chemotherapy
Volume60
Issue number3
Online published26 Feb 2016
Publication statusPublished - Mar 2016
Externally publishedYes

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.

Citation Format(s)

Mutational Analysis of Quinolone Resistance Protein QnrVC7 Provides Novel Insights into the Structure-Activity Relationship of Qnr Proteins. / Po, Kathy Hiu Laam; Chan, Edward Wai Chi; Chen, Sheng.

In: Antimicrobial Agents and Chemotherapy, Vol. 60, No. 3, 03.2016, p. 1939-1942.

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review