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Atrapar la proteína portadora de acilo dinámica en la biosíntesis de ácidos grasos
Chi Nguyen1, Robert W Haushalter2, D John Lee2
11] Departments of Molecular Biology and Biochemistry, Chemistry, and Pharmaceutical Sciences, University of California, Irvine, California 92697, USA [2].
Nature
|December 24, 2013
Resumen
La proteína portadora de acilo (ACP) estabiliza y transporta las cadenas lipídicas durante la biosíntesis de ácidos grasos. Un nuevo método de enlace cruzado revela la estructura compleja AcpP-FabA, mostrando la dinámica ACP crucial para la deshidratación y potencialmente aplicable a varias vías metabólicas.
Área de la Ciencia:
- Biología Estructural Biología estructural.
- La bioquímica es la bioquímica.
- Biología Molecular Biología Molecular
Sus antecedentes:
- La proteína portadora de acilo (ACP) es esencial para la biosíntesis de ácidos grasos, transportando los intermediarios de lípidos entre las enzimas.
- El estudio de las interacciones transitorias ACP-enzima es un desafío, lo que dificulta la comprensión estructural de alta resolución en la síntesis de ácidos grasos.
- Se necesita una nueva estrategia para investigar eficazmente estas interacciones proteína-proteína.
Objetivo del estudio:
- Desarrollar y aplicar una sonda basada en el mecanismo para el enlace cruzado covalente selectivo del sitio activo de AcpP (E. coli ACP) a FabA (deshidratasa de ácidos grasos).
- Para aclarar la base estructural de las interacciones ACP-enzima durante la biosíntesis de ácidos grasos.
- Comprender el mecanismo dinámico de la acción ACP en la deshidratación de los ácidos grasos.
Principales métodos:
- Mecanismo basado en el enlace cruzado de AcpP a FabA.
- Cristalografía de rayos X del complejo AcpP-FabA entrelazado a una resolución de 1.9 Å.
- Técnicas de resonancia magnética nuclear (RMN) de solución (perturbaciones de desplazamiento químico, acoplamientos dipolares residuales).
- Simulaciones de dinámica molecular.
Principales resultados:
- La estructura cristalina del complejo AcpP-FabA reveló un homodímero con AcpP en dos conformaciones distintas.
- Identificó los principales residuos interfaciales y los validó utilizando RMN, apoyando las interpretaciones estructurales.
- El FabA demostrado extruye la cadena acil desde el bolsillo de unión ACP antes de la deshidratación a través del reposicionamiento de la hélice III.
Conclusiones:
- El estudio proporciona la primera visión estructural y dinámica de ACP en acción durante la deshidratación de los ácidos grasos.
- La estrategia de enlaces cruzados desarrollada permite un estudio efectivo de las interacciones transitorias ACP-enzima.
- Las ideas sobre la dinámica de los países ACP pueden ser ampliamente aplicables a los ácidos grasos, los policetidos y la biosíntesis no ribosómica, lo que afecta a la investigación de enfermedades metabólicas.
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