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Orientation of the putative recognition helix in the DNA-binding domain of Hin recombinase complexed with the hix site.
Mack, D P; Sluka, J P; Shin, J A; Griffin, J H; Simon, M I; Dervan, P B.
Afiliação
  • Mack DP; Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena 91125.
Biochemistry ; 29(28): 6561-7, 1990 Jul 17.
Article em En | MEDLINE | ID: mdl-2204416
ABSTRACT
On the basis of sequence similarity with other known DNA-binding proteins, the DNA-binding domain of Hin recombinase, residues 139-190, is thought to bind DNA by a helix-turn-helix motif. Two models can be considered that differ in the orientation of the recognition helix in the major groove of DNA. One is based on the orientation of the recognition helix found in the 434 repressor (1-69) and lambda repressor-DNA cocrystals, and the other is based on the NMR studies of lac repressor headpiece. Cleavage by EDTA.Fe attached to a lysine side chain (Ser183----Lys183) near the COOH terminus of Hin(139-184) reveals that the putative recognition helix is oriented toward the center of the inverted repeats in a manner similar to that seen in the 434 and lambda repressor-DNA cocrystals.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / DNA Bacteriano / Proteínas de Ligação a DNA / DNA Nucleotidiltransferases Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 1990 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / DNA Bacteriano / Proteínas de Ligação a DNA / DNA Nucleotidiltransferases Tipo de estudo: Prognostic_studies Idioma: En Ano de publicação: 1990 Tipo de documento: Article