The solution structure of ParD, the antidote of the ParDE toxin-antitoxin module, provides the structural basis for DNA and toxin binding

Protein Science

Volumn 16, Issue 8, 2007, Pages 1676-1688

  Oberer, Monika ^a   Zangger, Klaus ^a   Gruber, Karl ^a   Keller, Walter ^a  

^a UNIVERSITY OF GRAZ   (Austria)

Author keywords

Bacterial programmed cell death; Homodimeric protein; Intermonomer NOEs; NMR spectroscopy; Ribbon helix helix; Toxin antitoxin systems

Indexed keywords

ANTIDOTE; ANTITOXIN; BACTERIAL PROTEIN; BACTERIAL TOXIN; HELIX LOOP HELIX PROTEIN; PROTEIN PARD; PROTEIN PARDE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DNA BINDING; ENZYME ACTIVATION; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OPERON; PLASMID; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BACTERIAL PROTEINS; BACTERIAL TOXINS; BASE SEQUENCE; BINDING SITES; DNA; DNA-BINDING PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PLASMIDS; PROTEIN STRUCTURE, TERTIARY; SOLUTIONS; STRUCTURE-ACTIVITY RELATIONSHIP;

BACTERIA (MICROORGANISMS);

EID: 34547564386     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062680707     Document Type: Article

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