1wap | pdb_00001wap
From Proteopedia
TRP RNA-BINDING ATTENUATION PROTEIN IN COMPLEX WITH L-TRYPTOPHAN
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Structural highlights
Function[MTRB_BACSU] Required for transcription attenuation control in the Trp operon. This trans-acting factor seems to recognize a 10 bases nucleotide sequence in the Trp leader transcript causing transcription termination. Binds the leader RNA only in presence of L-tryptophan.[1] Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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. The structure of trp RNA-binding attenuation protein.,Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P Nature. 1995 Apr 20;374(6524):693-700. PMID:7715723[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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