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The structure of trp RNA-binding attenuation protein

Nature volume 374, pages 693–700 (1995)Cite this article

The crystal structure of the trp RNA-binding attenuation protein of Bacillus subtilis solved at 1.8 Å resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit β-sheets to form a β-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent β-sheets in the β-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan.

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Authors and Affiliations

  1. Department of Chemistry, University of York, York, Y01 5DD, UK

    Alfred A. Antson, Andrzej M. Brzozowski, Eleanor J. Dodson, G. Guy Dodson & Keith S. Wilson

  2. Department of Biological Sciences, Cooke Hall State University of New York at Buffalo, Buffalo, New York, 14260, USA

    John Otridge, Thomas M. Smith, Min Yang, Tomasz Kurecki & Paul Gollnick

  3. European Molecular Biology Laboratory (EMBL), c/o DESY, Notkestrasse 85, 22603, Hamburg, Germany

    Keith S. Wilson

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Antson, A., Otridge, J., Brzozowski, A. et al. The structure of trp RNA-binding attenuation protein. Nature 374, 693–700 (1995). https://doi.org/10.1038/374693a0

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