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Estructura y mecanismo molecular de una familia de transportadores nucleobase-cation-symport-1
Simone Weyand1, Tatsuro Shimamura, Shunsuke Yajima
1Membrane Protein Laboratory, Diamond Light Source Limited, Harwell Science and Innovation Campus, Chilton, Didcot, Oxfordshire OX11 0DE, UK.
Science (New York, N.Y.)
|October 18, 2008
Resumen
El nucleobase-cation-symport-1 (NCS1) transportador es el transportador Mhp1
Área de la Ciencia:
- Biología Estructural Biología estructural.
- Transporte de la membrana Transporte de la membrana
- La bioquímica es la bioquímica.
Sus antecedentes:
- Los transportadores nucleobase-cation-symport-1 (NCS1) son vitales para el rescate de las nucleobases.
- Comprender su relación estructura-función es clave para descifrar el transporte celular de metabolitos.
Objetivo del estudio:
- Para determinar la estructura de alta resolución del transportador Mhp1.
- Para aclarar el mecanismo de unión y transporte del sustrato en los transportadores NCS1.
Principales métodos:
- Cristalografía de rayos X con una resolución de 2,85 angstroms.
- Determinación de las conformaciones ocluidas abiertas hacia afuera y sujetas al sustrato de Mhp1.1.
Principales resultados:
- Se resolvió la estructura de 2.85 angstroms de Mhp1, un transportador de bencilo-hidantoína.
- Mhp1 comprende 12 hélices de transmembrana, con 10 en repeticiones invertidas.
- Los cambios estructurales revelan cómo la cavidad orientada hacia el exterior se cierra al unirse el sustrato.
Conclusiones:
- La estructura de Mhp1 proporciona información sobre el mecanismo de acceso alternativo de los transportadores NCS1.
- La disposición simétrica de las cavidades y los movimientos sincronizados de las hélices explican la dinámica del transporte.
- Este trabajo sienta las bases para la comprensión de las proteínas de transporte de membrana relacionadas.
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