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Caracterización estructural del sitio de zinc en la proteína farnesiltransferasa
Daniel A Tobin1, Jennifer S Pickett, Heather L Hartman
1Department of Chemistry and Biophysics Research Division, The University of Michigan, Ann Arbor, MH 48109-1055, USA.
Journal of the American Chemical Society
|August 14, 2003
Resumen
La espectroscopia de absorción de rayos X revela la estructura del sitio de zinc (Zn) en la proteína farnesiltransferasa. Cambios en la ligadura al unirse al sustrato del péptido, lo que indica un papel en el mecanismo catalítico de la enzima.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- Biología Estructural Biología estructural.
- La espectroscopia es una técnica de espectroscopia.
Sus antecedentes:
- La proteína farnesiltransferasa (FTasa) es crucial para la prenilación de las proteínas.
- Comprender la estructura y la dinámica del sitio de zinc (Zn) es clave para dilucidar el mecanismo catalítico de la FTasa.
Objetivo del estudio:
- Para determinar la estructura del sitio de Zn en FTase utilizando espectroscopia de absorción de rayos X.
- Investigar cómo la unión al sustrato afecta la coordinación de Zn y la actividad de la FTasa.
Principales métodos:
- Se empleó la espectroscopia de estructura fina de absorción de rayos X extendida (EXAFS).
- El análisis se centró en las distancias del ligando Zn y el entorno de coordinación.
Principales resultados:
- Los datos de EXAFS indican que el Zn está ligado a tres átomos de bajo Z (N/O) y un átomo de cisteína sulfuro.
- La coordinación de Zn permanece en cuatro coordenadas al unirse al sustrato del péptido, cambiando de ZnS(N/O) 3 a ZnS2(N/O) 2.
- La formación del complejo del producto devuelve el Zn a su estado inicial de ligadura ZnS(N/O) 3.
Conclusiones:
- El estudio proporciona evidencia espectroscópica de cambios estructurales en el sitio de Zn durante la catálisis de la FTasa.
- Los cambios de ligadura observados sugieren que la cisteína C-terminal juega un papel en la unión al sustrato y la catálisis.
- El mecanismo catalítico de la FTasa implica cambios dinámicos en la esfera de coordinación del Zn.
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