2bx9
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(New page: 200px<br /> <applet load="2bx9" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bx9, resolution 2.80Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 18:18, 29 October 2007
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CRYSTAL STRUCTURE OF B.SUBTILIS ANTI-TRAP PROTEIN, AN ANTAGONIST OF TRAP-RNA INTERACTIONS
Overview
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 ... [(full description)]
About this Structure
2BX9 is a [Single protein] structure of sequence from [Bacillus subtilis] with ZN as [ligand]. Full crystallographic information is available from [OCA].
Reference
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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