The structure of Ap4A hydrolase complexed with ATP-MgFx reveals the basis of substrate binding

Structure

Volumn 10, Issue 2, 2002, Pages 205-213

  Fletcher, Jamie I ^a   Swarbrick, James D ^a   Maksel, Danuta ^a   Gayler, Kenwyn R ^a   Gooley, Paul R ^a  

^a UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

Ap4A hydrolase; Inhibitor; NMR spectroscopy; Nudix; Protein structure

Indexed keywords

ADENOSINE TRIPHOSPHATE MAGNESIUM; HYDROLASE;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; ENZYME BINDING; ENZYME STRUCTURE; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; ENZYME SUBUNIT; HEAT SHOCK; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN TARGETING;

ACID ANHYDRIDE HYDROLASES; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; ENZYME ACTIVATION; FLUORIDES; HUMANS; MAGNESIUM COMPOUNDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY;

BACTERIA (MICROORGANISMS); LUPINUS; LUPINUS ANGUSTIFOLIUS;

EID: 0036174723     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(02)00696-2     Document Type: Article

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