Structural highlights
Function
[RTPA_BACSU] By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP.
Publication Abstract from PubMed
In Bacillus subtilis the anti-TRAP protein (AT) is produced in response to the accumulation of uncharged tRNA(Trp). AT regulates expression of genes involved in tryptophan biosynthesis and transport by binding to the tryptophan-activated trp RNA-binding attenuation protein (TRAP) and preventing its interaction with several mRNAs. Here, we report the x-ray structure of AT at 2.8 angstroms resolution, showing that the protein subunits assemble into tight trimers. Four such trimers are further associated into a 12-subunit particle in which individual trimers are related by twofold and threefold symmetry axes. Twelve DnaJ-like, cysteine-rich zinc-binding domains form spikes on the surface of the dodecamer. Available data suggest several possible ways for AT to interact with the 11-subunit TRAP. Interaction between the two symmetry-mismatching molecules could be assisted by the flexible nature of AT zinc-binding domains.
Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction.,Shevtsov MB, Chen Y, Gollnick P, Antson AA Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17600-5. Epub 2005 Nov 23. PMID:16306262[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Shevtsov MB, Chen Y, Gollnick P, Antson AA. Crystal structure of Bacillus subtilis anti-TRAP protein, an antagonist of TRAP/RNA interaction. Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17600-5. Epub 2005 Nov 23. PMID:16306262 doi:0508728102
