LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Homologous_superfamily |
| Description | The tryptophan RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in Bacillus sp. by binding to the leader region of the nascent trp operon mRNA [ ]. The crystal structure of the Trp RNA-binding attenuation protein of Bacillus subtilis (mtrB, ) has been solved [ ]. TRAP forms an oligomeric ring consisting of 11 single-domain subunits, where each subunit adopts a double-stranded β-helix structure with the appearance of a β-sandwich of distinct architecture and jelly-roll fold. The 11 subunits are stabilised by 11 inter-subunit strands, forming a β-wheel with a large central hole. TRAP is activated by binding to tryptophan in clefts between adjacent β-strands, which induces conformational changes in the protein. Activated TRAP binds an mRNA target sequence consisting of 11 (G/U)AG repeats, separated by 2-3 spacer nucleotides. The spacer nucleotides do not make direct contact with the TRAP protein, but they do influence the conformation of the RNA, which might influence the specificity of TRAP [].This superfamily represents a domain with a TRAP-like double-stranded β-helix topology. This domain is found in TRAP proteins, as well as in the hypothetical protein SPyM3_0169 from Streptococcus pyogenes. SPyM3_0169 contains 9 domains per ring-like trimer, where each subunit contains three structural repeats. |
| Short Name | Trp_RNA-bd_attenuator-like_dom |
