喹诺酮耐药蛋白QnrVC7的突变分析为Qnr蛋白的构效关系提供了新见解。
Mutational Analysis of Quinolone Resistance Protein QnrVC7 Provides Novel Insights into the Structure-Activity Relationship of Qnr Proteins.
作者信息
Po Kathy Hiu Laam, Chan Edward Wai Chi, Chen Sheng
机构信息
Shenzhen Key Lab for Food Biological Safety Control, Food Safety and Technology Research Center, Hong Kong Polytechnic University Shenzhen Research Institute, Shenzhen, People's Republic of China State Key Lab of Chirosciences, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, People's Republic of China.
Shenzhen Key Lab for Food Biological Safety Control, Food Safety and Technology Research Center, Hong Kong Polytechnic University Shenzhen Research Institute, Shenzhen, People's Republic of China State Key Lab of Chirosciences, Department of Applied Biology and Chemical Technology, The Hong Kong Polytechnic University, Hung Hom, Kowloon, Hong Kong, People's Republic of China
出版信息
Antimicrob Agents Chemother. 2016 Jan 11;60(3):1939-42. doi: 10.1128/AAC.01805-15.
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.
本研究通过诱变研究评估了喹诺酮耐药蛋白QnrVC7串联重复环面4中位于i(-2)位置的残基的功能重要性。不同卷曲上的面4的i(-2)位置需要具有不同性质的残基。一些取代降低了QnrVC7的保护活性，而其中一些则提高了该活性。这些发现增进了我们对Qnr蛋白详细结构组织和功能要求的理解。
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