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A novel endonuclease mechanism directly visualized for I-PpoI.
Galburt, E A; Chevalier, B; Tang, W; Jurica, M S; Flick, K E; Monnat, R J; Stoddard, B L.
Afiliación
  • Galburt EA; Fred Hutchinson Cancer Research Center and the Graduate Programs in Molecular and Cell Biology and Biomolecular Structure and Design, University of Washington, 1100 Fairview Ave. N. A3-023, Seattle, Washington 98109, USA.
Nat Struct Biol ; 6(12): 1096-9, 1999 Dec.
Article en En | MEDLINE | ID: mdl-10581547
A novel mechanism of DNA endonucleolytic cleavage has been visualized for the homing endonuclease I-PpoI by trapping the uncleaved enzyme-substrate complex and comparing it to the previously visualized product complex. This enzyme employs a unique single metal mechanism. A magnesium ion is coordinated by an asparagine residue and two DNA oxygen atoms and stabilizes the phosphoanion transition state and the 3'oxygen leaving group. A hydrolytic water molecule is activated by a histidine residue for an in-line attack on the scissile phosphate. A strained enzyme-substrate-metal complex is formed before cleavage, then relaxed during the reaction.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Physarum polycephalum / Endodesoxirribonucleasas Límite: Animals Idioma: En Revista: Nat Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 1999 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Buscar en Google
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Physarum polycephalum / Endodesoxirribonucleasas Límite: Animals Idioma: En Revista: Nat Struct Biol Asunto de la revista: BIOLOGIA MOLECULAR Año: 1999 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos