The src homology 3-like domain of the diphtheria toxin repressor (DtxR) modulates repressor activation through interaction with the ancillary metal ion-binding site

Journal of Bacteriology

Volumn 185, Issue 7, 2003, Pages 2251-2258

  Love, John F ^a   VanderSpek, Johanna C ^a   Murphy, John R ^a,b  

^a BOSTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2,2' BIPYRIDINE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; DIPHTHERIA TOXIN; IRON; METAL ION; REPRESSOR PROTEIN; SOLVENT;

ARTICLE; BINDING SITE; CONTROLLED STUDY; CORYNEBACTERIUM DIPHTHERIAE; ELECTROPHORETIC MOBILITY; GENE; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; MUTANT; MUTATION; NONHUMAN; PHENOTYPE; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION;

AMINO ACID SUBSTITUTION; ANILINO NAPHTHALENESULFONATES; BACTERIAL PROTEINS; BINDING SITES; CATIONS; CORYNEBACTERIUM DIPHTHERIAE; DNA-BINDING PROTEINS; ESCHERICHIA COLI; FLUORESCENT DYES; GENE EXPRESSION REGULATION, BACTERIAL; METALS; MUTATION; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; REPRESSOR PROTEINS; SRC HOMOLOGY DOMAINS;

ACTINOBACTERIA (CLASS); CORYNEBACTERIUM; CORYNEBACTERIUM DIPHTHERIAE; UNCULTURED ACTINOMYCETE;

EID: 0037377828     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.7.2251-2258.2003     Document Type: Article

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