Analysis of internal motions of RNase T1 complexed with a productive substrate involving 15N NMR relaxation measurements.
J Biochem
; 140(1): 43-8, 2006 Jul.
Article
en En
| MEDLINE
| ID: mdl-16877767
ABSTRACT
The backbone dynamics of RNase T1 in the presence of exo-guanosine 2',3'-cyclophosphorothioate (exo-cGPS isomer), which is a productive substrate, and in the presence of 3'-guanylic acid (3'GMP), which is an nonproductive substrate, were examined using (15)N nuclear magnetic resonance. Although the X-ray crystal structure suggests that the modes of binding of these substrates to the active-site cleft are very similar, the order parameters in a number of regions in RNase T1 complexed with exo-cGPS isomer were different from those with 3'GMP. Moreover, the chemical exchange in line width observed for RNase T1 complexed with exo-cGPS isomer was also different from that observed for RNase T1 complexed with 3'GMP. From these results, we concluded that the internal motions in RNase T1 complexed with a productive substrate were not always identical to those in RNase T1 complexed with a nonproductive substrate.
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Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Tionucleótidos
/
Ribonucleasa T1
/
GMP Cíclico
/
Guanosina Monofosfato
Idioma:
En
Revista:
J Biochem
Año:
2006
Tipo del documento:
Article