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Crystal structure of a microbial ribonuclease, RNase St

Nature volume 299, pages 564–566 (1982)Cite this article

Abstract

The existence of a group of microbial RNases that hydrolyse 3′, 5′-phosphodiester linkages of RNA with a mechanism similar to that of pancreatic RNase A has long been known1. There is a rather poor homology between the six known primary sequences of these enzymes (Table 1), but the alignment around the possible functional residues may be systematic. There seems to be no homology at all between the primary sequences of these RNases and those2 of pancreatic RNases. The three-dimensional structure of RNase has been determined only for one member of the latter group, bovine pancreatic RNase A3,4 and its derivative, RNase S5,6. Here we report the three-dimensional structure of a microbial ribonuclease, RNase St, determined by the isomorphous replacement method. Both the polypeptide chain folding (reported earlier)7 and the active site environment are completely different from those of RNase A (or S), while they bear partial resemblance to those of barnase8 (a ribonuclease from Bacillus amyloliquefaciens).

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Author notes

  1. Kazuyuki Iwahashi

    Present address: Central Research Institute, Kyowa Hakko Co. Ltd, Machida, Tokyo, 194, Japan

  2. Nobuo Yoshida: Shionogi Research Laboratory, Shionogi and Co. Ltd, Fukushimaku, Osaka 553, Japan

Authors and Affiliations

  1. Faculty of Pharmaceutical Sciences, University of Tokyo, Hongo, Tokyo, 113, Japan

    Kazuo T. Nakamura, Kazuyuki Iwahashi, Yoshio Yamamoto, Yoichi Iitaka, Nobuo Yoshida & Yukio Mitsui

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  1. Kazuo T. Nakamura
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  2. Kazuyuki Iwahashi
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  3. Yoshio Yamamoto
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  4. Yoichi Iitaka
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  5. Nobuo Yoshida
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  6. Yukio Mitsui
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Nakamura, K., Iwahashi, K., Yamamoto, Y. et al. Crystal structure of a microbial ribonuclease, RNase St. Nature 299, 564–566 (1982). https://doi.org/10.1038/299564a0

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