Please use this identifier to cite or link to this item: http://hdl.handle.net/10397/61042
Title: Mutational analysis of quinolone resistance protein QnrVC7 provides novel insights into the structure-activity relationship of Qnr proteins
Authors: Po, KHL
Chan, EWC
Chen, S 
Issue Date: 2016
Publisher: American Society for Microbiology
Source: Antimicrobial agents and chemotherapy, 2016, v. 60, no. 3, p. 1939-1942 How to cite?
Journal: Antimicrobial agents and chemotherapy 
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.
URI: http://hdl.handle.net/10397/61042
ISSN: 0066-4804 (print)
1098-6596 (online)
DOI: 10.1128/AAC.01805-15
Appears in Collections:Journal/Magazine Article

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