The structure of Clostridium difficile toxin A glucosyltransferase domain bound to Mn 2+ and UDP provides insights into glucosyltransferase activity and product release

FEBS Journal

Volumn 279, Issue 17, 2012, Pages 3085-3097

  D'Orzo, Nunzia ^a   Malito, Enrico ^a   Biancucci, Marco ^a   Bottomley, Matthew J ^a   Maione, Domenico ^a   Scarselli, Maria ^a   Martinelli, Manuele ^a  

^a NOVARTIS VACCINES AND DIAGNOSTICS   (Italy)

Author keywords

glucosyl hydrolase activity; large clostridial toxins; TcdA structure

Indexed keywords

AMMONIA; CLOSTRIDIUM DIFFICILE TOXIN A; GLUCOSE; GLUCOSYLTRANSFERASE; MANGANESE; POTASSIUM; URIDINE DIPHOSPHATE GLUCOSE;

ARTICLE; BREVIBACILLUS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; THERMOSTABILITY; WILD TYPE;

BACTERIAL TOXINS; CLOSTRIDIUM DIFFICILE; ENTEROTOXINS; ENZYME ACTIVATION; GLYCOSYLTRANSFERASES; HYDROLYSIS; MANGANESE; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; QUATERNARY AMMONIUM COMPOUNDS; URIDINE DIPHOSPHATE;

BREVIBACILLUS; CLOSTRIDIUM DIFFICILE;

EID: 84865250349     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08688.x     Document Type: Article

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