1WAP

TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN

Summary for 1WAP

• Entry DOI: 10.2210/pdb1wap/pdb
• Descriptor: TRP RNA-BINDING ATTENUATION PROTEIN, TRYPTOPHAN (3 entities in total)
• Functional Keywords: trp operon, bacillus subtilis, rna-binding attenuation protein
• Biological source: Bacillus subtilis
• Total number of polymer chains: 22
• Total formula weight: 188049.49

Authors

Antson, A.A.,Dodson, E.J.,Gollnick, P. (deposition date: 1995-02-03, release date: 1995-06-03, Last modification date: 2024-02-14)

Primary citation

Antson, A.A.,Otridge, J.,Brzozowski, A.M.,Dodson, E.J.,Dodson, G.G.,Wilson, K.S.,Smith, T.M.,Yang, M.,Kurecki, T.,Gollnick, P.
The structure of trp RNA-binding attenuation protein.
Nature, 374:693-700, 1995

PubMed 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.

PubMed: 7715723
DOI: 10.1038/374693a0

Experimental method

X-RAY DIFFRACTION (1.8 Å)