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Nature. 1995 Apr 20;374(6524):693-700.

The structure of trp RNA-binding attenuation protein.

Author information

1
Department of Chemistry, University of York, UK.

Abstract

The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-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.

PMID:
7715723
DOI:
10.1038/374693a0
[Indexed for MEDLINE]

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