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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.
Afiliação
  • Po KH; 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.
  • Chan EW; 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.
  • Chen S; 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 sheng.chen@polyu.edu.hk.
Antimicrob Agents Chemother ; 60(3): 1939-42, 2016 Jan 11.
Article em En | MEDLINE | ID: mdl-26824937
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.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Relação Estrutura-Atividade / Ciprofloxacina / Proteínas de Escherichia coli / Farmacorresistência Bacteriana / Escherichia coli / Antibacterianos Idioma: En Revista: Antimicrob Agents Chemother Ano de publicação: 2016 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Relação Estrutura-Atividade / Ciprofloxacina / Proteínas de Escherichia coli / Farmacorresistência Bacteriana / Escherichia coli / Antibacterianos Idioma: En Revista: Antimicrob Agents Chemother Ano de publicação: 2016 Tipo de documento: Article