Three-dimensional structure of the DNA-binding domain of the fructose repressor from Escherichia coli by 1H and 15N NMR

Journal of Molecular Biology

Volumn 270, Issue 3, 1997, Pages 496-510

  Penin, François ^a   Geourjon, Christophe ^a   Montserret, Roland ^a   Böckmann, Anja ^a,d   Lesage, Anne ^a,c   Yang, Yin Shan ^a,b   Bonod Bidaud, Christelle ^a   Cortay, Jean Claude ^a   Nègre, Didier ^a   Cozzone, Alain J ^a   Deléage, Gilbert ^a  

^a CNRS   (France)

^b CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^c UNIVERSITÉ DE LYON   (France)

^d Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

DNA binding domain; fru repressor; Helix turn helix motif; Heteronuclear NMR spectroscopy; Protein structure

Indexed keywords

BACTERIAL PROTEIN; DNA BINDING PROTEIN; FRUCTOSE; NITROGEN 15; REPRESSOR PROTEIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONTROLLED STUDY; ESCHERICHIA COLI; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR MODEL; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DNA BINDING; PROTEIN FAMILY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; STEREOCHEMISTRY; TRANSCRIPTION REGULATION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0031577341     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1123     Document Type: Article

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