High resolution structures of the human ABO(H) blood group enzymes in complex with donor analogs reveal that the enzymes utilize multiple donor conformations to bind substrates in a stepwise manner

Journal of Biological Chemistry

Volumn 290, Issue 45, 2015, Pages 27040-27052

  Gagnon, Susannah M L ^a   Meloncelli, Peter J ^b   Zheng, Ruixiang B ^b   Haji Ghassemi, Omid ^a   Johal, Asha R ^a   Borisova, Svetlana N ^a   Lowary, Todd L ^b   Evans, Stephen V ^a  

^a UNIVERSITY OF VICTORIA   (Canada)

^b UNIVERSITY OF ALBERTA   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; SUBSTRATES;

DONOR BINDING; GLYCOSYL TRANSFERASE; HIGH RESOLUTION; HIGH-RESOLUTION STRUCTURES; MULTISTAGE PROCESS; STRUCTURAL INVESTIGATION; SUBSTRATE BINDING; SUBSTRATE HYDROLYSIS;

BINS;

ALPHA 1,3 GALACTOSYLTRANSFERASE; ALPHA 1,3 N ACETYLGALACTOSAMINYLTRANSFERASE; GALACTOSE; N ACETYLGALACTOSAMINYLTRANSFERASE; UDP PHOSPHONOGALACTOSE; UNCLASSIFIED DRUG; URACIL; BLOOD GROUP ABO SYSTEM; GALACTOSYLTRANSFERASE; HYBRID PROTEIN; N-ACETYLLACTOSAMINIDE ALPHA-1,3-GALACTOSYLTRANSFERASE;

ARTICLE; BINDING AFFINITY; BINDING SITE; BLOOD GROUP ABO SYSTEM; CATALYSIS; CHIMERA; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ASSAY; ENZYME CONFORMATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; HUMAN; HYDROGEN BOND; MOLECULAR DYNAMICS; PRIORITY JOURNAL; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; CHEMISTRY; ENZYME ACTIVE SITE; GENETICS; HYDROLYSIS; METABOLISM; MOLECULAR MIMICRY; MOLECULAR MODEL; PROTEIN CONFORMATION; SEQUENCE HOMOLOGY; STATIC ELECTRICITY; STEREOISOMERISM; X RAY CRYSTALLOGRAPHY;

ABO BLOOD-GROUP SYSTEM; AMINO ACID SEQUENCE; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; GALACTOSYLTRANSFERASES; HUMANS; HYDROGEN BONDING; HYDROLYSIS; MODELS, MOLECULAR; MOLECULAR MIMICRY; N-ACETYLGALACTOSAMINYLTRANSFERASES; PROTEIN CONFORMATION; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STATIC ELECTRICITY; STEREOISOMERISM; SUBSTRATE SPECIFICITY;

EID: 84946779761     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.682401     Document Type: Article

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