Three‐dimensional structure of ribonuclease Ms*3′‐guanylic acid complex at 2.5 Å resolution

FEBS Letters

Mitsui, Yukio²  Nakamura, Kazuo T.²  Nonaka, Takamasa²  Irie, Masachika¹ 

[1] Department of Microbiology, Hoshi College of Pharmacy, Shinagawa-ku, Tokyo 142, Japan;Faculty of Engineering, Nagaoka University of Technology, Nagaoka, Niigata 940-21, Japan

关键词: Ribonuclease Ms;    Inhibitor;    Crystal structure;    Aspergillus saitol;    RNase;    ribonuclease;    3′-GMP;    3′-guanylic acid;    2′-GMP;    2′-guanylic acid;    r.m.s;    root-mean-square;   

DOI  :  10.1016/0014-5793(91)80589-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The crystal structure of ribonuclease Ms*3⁺-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 T₁*2′-guanylic acid complex. As for the possible general base in the trans-phosphorylation step of the catalysis, 0 c 1 of Glu¹⁷ is within the hydrogen-bond distance (2.7 Å) of the 2′-0 of the nucleotide while N c 2 of His¹⁴ is significantly more distant (3.4 Å) from the 2′-0.

【 授权许可】

Unknown