Abstract
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 language | English |
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Pages (from-to) | 1939-1942 |
Number of pages | 4 |
Journal | Antimicrobial Agents and Chemotherapy |
Volume | 60 |
Issue number | 3 |
DOIs | |
Publication status | Published - 1 Mar 2016 |
ASJC Scopus subject areas
- Pharmacology
- Pharmacology (medical)
- Infectious Diseases