Nonaka T, Mitsui Y, Irie M, Nakamura K T
Faculty of Engineering, Nagaoka University of Technology, Niigato, Japan.
FEBS Lett. 1991 Jun 3;283(2):207-9. doi: 10.1016/0014-5793(91)80589-u.
The crystal structure of ribonuclease Ms3'-guanylic acid complex has been determined by molecular replacement methods based on the known structure of ribonuclease T1. The pattern of hydrogen-bonds between the enzyme and the guanine base is similar to that discovered by Arni et al. [( 1988) J. Biol. Chem. 263, 15358-15368] in the crystal structure of ribonuclease T12'-guanylic acid complex. As for the possible general base in the trans-phosphorylation step of the catalysis, 0 epsilon 1 of Glu57 is within the hydrogen-bond distance (2.7 A) of the 2'-0 of the nucleotide while N epsilon 2 of His39 is significantly more distant (3.4 A) from the 2'-0.
基于核糖核酸酶T1的已知结构,通过分子置换法确定了核糖核酸酶Ms3'-鸟苷酸复合物的晶体结构。该酶与鸟嘌呤碱基之间的氢键模式类似于Arni等人[(1988年)《生物化学杂志》263, 15358 - 15368]在核糖核酸酶T12'-鸟苷酸复合物晶体结构中发现的模式。至于催化转磷酸化步骤中可能的通用碱,Glu57的Oε1在核苷酸2'-O的氢键距离(2.7 Å)内,而His39的Nε2与2'-O的距离明显更远(3.4 Å)。