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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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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DOI: https://doi.org/10.1038/297162a0
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