Structural and mechanistic insight into covalent substrate binding by Escherichia coli dihydroxyacetone kinase

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

Volumn 108, Issue 4, 2011, Pages 1302-1307

  Shi, Rong ^a   McDonald, Laura ^b   Cui, Qizhi ^c   Matte, Allan ^c   Cygler, Miroslaw ^a,c   Ekiel, Irena ^b,c  

^a MCGILL UNIVERSITY   (Canada)

^b Dept of Electrical and Computer Engineering   (Canada)

^c NATIONAL RESEARCH COUNCIL CANADA   (Canada)

Author keywords

DhaK DhaL complex; Kinase mechanism

Indexed keywords

BACTERIAL ENZYME; DIHYDROXYACETONE KINASE K; DIHYDROXYACETONE KINASE L; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

ARTICLE; COMPLEX FORMATION; COVALENT BOND; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL;

AMINO ACID SUBSTITUTION; BINDING SITES; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; MUTATION; PHOSPHOTRANSFERASES (ALCOHOL GROUP ACCEPTOR); PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; SUBSTRATE SPECIFICITY;

BUTEA MONOSPERMA; ESCHERICHIA COLI;

EID: 79952139700     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1012596108     Document Type: Article

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