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Molecular structure of a new family of ribonucleases

Nature volume 297, pages 162–164 (1982)Cite this article

Abstract

Bacillus amyloliquefaciens produces a ribonuclease1 (barnase), the function of which is probably the digestion of external RNA: it is excreted by the bacillus and within the cell its action is inhibited by a protein of ∼89 residues to which it binds with high affinity2. Determination3 of the amino acid sequence of the ribonuclease, which is a monomer of molecular weight 12,382 consisting of 110 residues, has revealed its homology with other prokaryotic and eukaryotic ribonucleases4–6. We have now determined the atomic structure of barnase by X-ray crystallographic analysis. We report that its structure includes a large central β-pleated sheet and two α-helices. The arrangement of these secondary structures is different from that found in bovine pancreatic ribonuclease.

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Author notes

  1. G. Bricogne

    Present address: Department of Biochemistry, Columbia University College of Physicians and Surgeons, 630 West 168 Street, New York, New York, 10032, USA

  2. A. Jack: Deceased

Authors and Affiliations

  1. Centre Pharmaceutique et LURE, Université Paris-Sud, Chatenay-Malabry, 92290, France

    Y. Mauguen

  2. Laboratory of Nutrition and Endocrinology, National Institute of Arthritis, Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland, 20205, USA

    Robert W. Hartley

  3. Department of Chemistry, University of York, Heslington, York, YO1 5DD, UK

    E. J. Dodson & G. G. Dodson

  4. MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK

    G. Bricogne, Cyrus Chothia & A. Jack

Authors
  1. Y. Mauguen
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Mauguen, Y., Hartley, R., Dodson, E. et al. Molecular structure of a new family of ribonucleases. Nature 297, 162–164 (1982). https://doi.org/10.1038/297162a0

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