2bx9
CRYSTAL STRUCTURE OF B.SUBTILIS ANTI-TRAP PROTEIN, AN ANTAGONIST OF TRAP-RNA INTERACTIONS
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OverviewOverview
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.
About this StructureAbout this Structure
2BX9 is a Single protein structure of sequence from Bacillus subtilis with ZN as ligand. Structure known Active Site: AC1. Full crystallographic information is available from OCA.
ReferenceReference
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
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