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Voltear inducido por la luz de una cadena lateral de glutamina conservada y su orientación en el dominio AppA BLUF
Jeffrey S Grinstead1, Marcela Avila-Perez, Klaas J Hellingwerf
1Department of NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Journal of the American Chemical Society
|November 23, 2006
Resumen
El fotorreceptor de luz azul AppA.
Área de la Ciencia:
- La bioquímica es la bioquímica.
- La fotoquímica es la fotoquímica.
- Biología Molecular Biología Molecular
Sus antecedentes:
- El dominio AppA BLUF es un fotorreceptor de luz azul que contiene flavin.
- La glutamina 63 conservada es crítica para el fotociclo de AppA.
- Estudios previos sobre la orientación de la glutamina 63 dieron resultados contradictorios.
Objetivo del estudio:
- Para aclarar la orientación de la glutamina 63 en el fotociclo de la proteína AppA.
- Para proporcionar evidencia espectroscópica de cambios conformacionales inducidos por la luz.
Principales métodos:
- Se empleó la espectroscopia de Resonancia Magnética Nuclear (RMN).
- Los datos se compararon con los datos existentes de absorción UV / vis, FTIR y estructura cristalina.
Principales resultados:
- La espectroscopia de RMN confirmó el volteo inducido por la luz de la cadena lateral de la glutamina 63.
- Se forma un fuerte enlace de hidrógeno entre la glutamina 63 y la tirosina 21 en el estado inducido por la luz.
- Los hallazgos se alinean con los datos espectroscópicos y estructurales anteriores para AppA WT.
Conclusiones:
- La cadena lateral de la glutamina 63 sufre un cambio inducido por la luz en el dominio AppA BLUF.
- Este cambio conformacional es esencial para el mecanismo del fotociclo de la proteína.
- Los datos de RMN resuelven las discrepancias con respecto a la orientación de la glutamina 63.
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