The mutation G145S in PrfA, a key virulence regulator of Listeria monocytogenes, increases DNA-binding affinity by stabilizing the HTH motif

Molecular Microbiology

Volumn 56, Issue 2, 2005, Pages 433-446

  Eiting, Marina ^a   Hagelüken, Gregor ^a   Schubert, Wolf Dieter ^a   Heinz, Dirk W ^a  

^a HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP; HELIX LOOP HELIX PROTEIN; OXYGEN; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR PRFA; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BACTERIAL GENE; BACTERIAL STRAIN; BACTERIAL VIRULENCE; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; DNA BINDING; GENE MUTATION; GENE OVEREXPRESSION; GENE STRUCTURE; LISTERIA MONOCYTOGENES; NONHUMAN; PATHOGENICITY; PRFA GENE; PRIORITY JOURNAL; PROTEIN MOTIF; PROTEIN STABILITY; SURFACE PLASMON RESONANCE; WILD TYPE;

AMINO ACID MOTIFS; BACTERIAL PROTEINS; CYCLIC AMP RECEPTOR PROTEIN; DNA; DNA-BINDING PROTEINS; GENE EXPRESSION REGULATION, BACTERIAL; GENES, REGULATOR; HELIX-TURN-HELIX MOTIFS; LISTERIA MONOCYTOGENES; MUTATION; PEPTIDE TERMINATION FACTORS; SURFACE PLASMON RESONANCE; TRANS-ACTIVATORS; VIRULENCE;

LISTERIA MONOCYTOGENES; POSIBACTERIA;

EID: 17144398027     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2005.04561.x     Document Type: Article

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