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La estructura de la hélice beta y las propiedades de unión al hielo de una proteína anticongelante hiperactiva de un

S P Graether¹, M J Kuiper, S M Gagné

¹Department of Biochemistry, Queen's University, Kingston, Ontario, Canada.

|August 5, 2000

Resumen

Las proteínas anticongelantes de insectos (AFP) muestran una inhibición superior de los cristales de hielo en comparación con las AFP de peces o plantas. El gusano de las yemas de abeto AFP.

Área de la Ciencia:

La bioquímica es la bioquímica.
Biología Estructural Biología estructural.
Criobiología Criobiología.

Sus antecedentes:

Las proteínas anticongelantes de insectos (AFP) exhiben una inhibición del crecimiento de cristales de hielo significativamente mayor que las de peces o plantas.
Las AFP de insectos, también llamadas proteínas de histeresis térmica, son conocidas por sus potentes propiedades crioprotectoras.
Investigaciones anteriores han establecido la mayor eficacia de las AFP de insectos, algunas de las cuales son 10-100 veces más efectivas que las AFP de peces.

Objetivo del estudio:

Determinar la estructura de la solución de la proteína anticongelante (AFP) del gusano de los brotes de abeto (Choristoneura fumiferana).
Para caracterizar las propiedades de unión al hielo de este insecto AFP.
Para aclarar la base estructural para la mayor actividad de las AFPs de insectos.

Principales métodos:

Se utilizó la espectroscopia de Resonancia Magnética Nuclear (RMN) para determinar la estructura de la solución 3D del gusano de brotes de abeto AFP de 9 kDa.
La morfología de los cristales de hielo fue analizada usando microscopía.
Se realizaron experimentos de grabado de hielo para estudiar las interacciones AFP-hielo.

Principales resultados:

El gusano de brotes de abeto AFP adopta una estructura de beta-hélice con una sección transversal triangular, distinta de las estructuras conocidas de AFP de peces.
La superficie de unión del hielo presenta una serie de residuos de treonina (motivos TXT) que coinciden exactamente con la red de hielo en el prisma y los planos basales.
Los datos experimentales apoyan la unión de AFP tanto al prisma como a los planos basales de hielo.

Conclusiones:

La estructura única de la hélice beta y la disposición específica de los residuos de treonina en la cara de unión al hielo de la lombriz de abeto AFP explican su alta actividad inhibidora del hielo.
La capacidad de esta AFP de unirse a múltiples planos de hielo contribuye a su rendimiento superior en comparación con otras AFP.
Este estudio proporciona información estructural sobre los mecanismos crioprotectores mejorados de las proteínas anticongelantes de insectos.

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