volume 32, issue 44, P11825-11837 1993
DOI: 10.1021/bi00095a011
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Takamasa Nonaka, Kazuo T. Nakamura, Seiichi Uesugi, Morio Ikehara, Masachika Irie, Yukio Mitsui

Abstract: A ribonuclease T1 homologue, ribonuclease Ms (RNase Ms) from Aspergillus saitoi, has been crystallized as a complex with a substrate analogue GfpC where the 2'-hydroxyl (2'-OH) group of guanosine in guanylyl-3',5'-cytidine (GpC) is replaced by the 2'-fluorine (2'-F) atom to prevent transesterification. The crystal structure of the complex was solved at 1.8-A resolution to a final R-factor of 0.204. The role of His92 (RNase T1 numbering) as the general acid catalyst was confirmed. Of the two alternative candida…

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