Structural basis of rifampin inactivation by rifampin phosphotransferase

Proceedings of the National Academy of Sciences of the United States of America

Volumn 113, Issue 14, 2016, Pages 3803-3808

  Qi, Xiaofeng ^a,b   Lin, Wei ^a,d   Ma, Miaolian ^a   Wang, Chengyuan ^a,b   He, Yang ^a,b   He, Nisha ^a,b   Gao, Jing ^c   Zhou, Hu ^c   Xiao, Youli ^a   Wang, Yong ^a   Zhang, Peng ^a  

^a INSTITUTE OF PLANT PHYSIOLOGY AND ECOLOGY   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c SHANGHAI INSTITUTE OF MATERIA MEDICA   (China)

^d RUTGERS UNIVERSITY   (United States)

Author keywords

Antibiotic resistance; Molecular mechanism; Phosphotransferase; Rifampin; Toggle switch

Indexed keywords

1 NAPHTHOL; 2 NAPHTHOL; HYDROXYL GROUP; PHOSPHOTRANSFERASE; RIFAMPICIN; RIFAMPIN PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG; 2-NAPHTHOL; ADENOSINE TRIPHOSPHATE; NAPHTHOL DERIVATIVE; PROTEIN BINDING; SULFONIC ACID DERIVATIVE;

ARTICLE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DRUG INACTIVATION; DRUG MECHANISM; LISTERIA MONOCYTOGENES; NONHUMAN; PHOSPHATE TRANSPORT; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; ANTIBIOTIC RESISTANCE; BINDING SITE; CHEMISTRY; DRUG EFFECTS; ENZYME ACTIVE SITE; METABOLISM; MICROBIAL SENSITIVITY TEST; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY;

ADENOSINE TRIPHOSPHATE; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DRUG RESISTANCE, BACTERIAL; LISTERIA MONOCYTOGENES; MICROBIAL SENSITIVITY TESTS; NAPHTHOLS; PHOSPHOTRANSFERASES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RIFAMPIN; SULFONIC ACIDS;

EID: 84962626291     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1523614113     Document Type: Article

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