The wing of a winged helix-turn-helix transcription factor organizes the active site of BirA, a bifunctional repressor/ligase

Journal of Biological Chemistry

Volumn 288, Issue 50, 2013, Pages 36029-36039

  Chakravartty, Vandana ^a   Cronan, John E ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DELETERIOUS EFFECTS; DELETION MUTANTS; ENZYMATIC ACTIVITIES; ENZYMATIC REACTION; LIGASE ACTIVITY; PROTEIN LIGASE ACTIVITY; TRANSCRIPTIONAL REGULATION; TRANSCRIPTIONAL REGULATOR;

COENZYMES; ESCHERICHIA COLI; TRANSCRIPTION FACTORS;

BIOSYNTHESIS;

ADENOSINE DIPHOSPHATE; ADENOSINE PHOSPHATE; BIOTIN; BIOTIN DERIVATIVE; BIOTINOYL 5' ADENOSINE PHOSPHATE; BIRA PROTEIN; HELIX LOOP HELIX PROTEIN; MUTANT PROTEIN; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR OMPR; UNCLASSIFIED DRUG; WINGED HELIX TRANSCRIPTION FACTOR; WNT1 PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIAL GROWTH; BACTERIAL STRAIN; BIOTINYLATION; CHEMICAL REACTION; CHIMERA; CONTROLLED STUDY; DNA BINDING; DNA BINDING MOTIF; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME REPRESSION; ESCHERICHIA COLI; GENETIC COMPLEMENTATION; IN VITRO STUDY; MUTATIONAL ANALYSIS; NONHUMAN; OPERON; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEPLETION; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; TRANSCRIPTION REGULATION;

AMP; BACTERIAL GENETICS; BACTERIAL METABOLISM; ENZYME CATALYSIS; ENZYME MUTATION; MICROBIOLOGY; PROMOTERS; TRANSCRIPTION FACTORS; TRANSCRIPTION REGULATION; TRANSCRIPTION TARGET GENES;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BIOTINYLATION; CARBON-NITROGEN LIGASES; CATALYTIC DOMAIN; DNA; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; REPRESSOR PROTEINS; SEQUENCE DELETION; WINGED-HELIX TRANSCRIPTION FACTORS;

EID: 84890419305     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.525618     Document Type: Article

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