Sulfonation of glycopeptide antibiotics by sulfotransferase StaL depends on conformational flexibility of aglycone scaffold

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

Volumn 109, Issue 29, 2012, Pages 11824-11829

  Shi, Rong ^a   Munger, Christine ^a   Kalan, Lindsay ^b   Sulea, Traian ^c   Wright, Gerard D ^b   Cygler, Miroslaw ^a,d  

^a MCGILL UNIVERSITY   (Canada)

^b MCMASTER UNIVERSITY   (Canada)

^c NATIONAL RESEARCH COUNCIL CANADA   (Canada)

^d UNIVERSITY OF SASKATCHEWAN   (Canada)

Author keywords

Substrate binding; Substrate flexibility; Substrate recognition

Indexed keywords

ADENOSINE 3',5' DIPHOSPHATE; ADENOSINE DERIVATIVE; AGLYCONE; ANTIBIOTIC AGENT; GLYCOPEPTIDE; HEPTAPEPTIDE; HISTIDINE; HYDROXYL GROUP; OXFENICINE; SULFOTRANSFERASE; SULFOTRANSFERASE STAL; TEICOPLANIN; UNCLASSIFIED DRUG; VANCOMYCIN;

ANTIBIOTIC RESISTANCE; ARTICLE; CONFORMATIONAL TRANSITION; CROSS LINKING; CRYSTAL STRUCTURE; ENZYME ACTIVE SITE; ENZYME MODIFICATION; ENZYME SUBSTRATE COMPLEX; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN ASSEMBLY; STEREOSPECIFICITY; SULFONATION;

ADENOSINE DIPHOSPHATE; ANTI-BACTERIAL AGENTS; CRYSTALLOGRAPHY; DRUG DISCOVERY; GLYCINE; HYDROGEN BONDING; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; PROTEIN CONFORMATION; RISTOCETIN; SULFOTRANSFERASES;

BACTERIA (MICROORGANISMS); POSIBACTERIA;

EID: 84863924678     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1205377109     Document Type: Article

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