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 PubMed
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.
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 Also
References
- ↑ Babitzke P, Gollnick P, Yanofsky C. The mtrAB operon of Bacillus subtilis encodes GTP cyclohydrolase I (MtrA), an enzyme involved in folic acid biosynthesis, and MtrB, a regulator of tryptophan biosynthesis. J Bacteriol. 1992 Apr;174(7):2059-64. PMID:1551827
- ↑ Antson AA, Otridge J, Brzozowski AM, Dodson EJ, Dodson GG, Wilson KS, Smith TM, Yang M, Kurecki T, Gollnick P. The structure of trp RNA-binding attenuation protein. Nature. 1995 Apr 20;374(6524):693-700. PMID:7715723 doi:http://dx.doi.org/10.1038/374693a0
