2fx0
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(New page: 200px<br /><applet load="2fx0" size="350" color="white" frame="true" align="right" spinBox="true" caption="2fx0, resolution 2.40Å" /> '''Crystal Structure of...)
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Revision as of 17:46, 29 January 2008
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Crystal Structure of HlyIIR, a Hemolysin II transcriptional Regulator
Overview
Production of Bacillus cereus and Bacillus anthracis toxins is controlled, by a number of transcriptional regulators. Here we report the crystal, structure of B. cereus HlyIIR, a regulator of the gene encoding the, pore-forming toxin hemolysin II. We show that HlyIIR forms a tight dimer, with a fold and overall architecture similar to the TetR family of, repressors. A remarkable feature of the structure is a large internal, cavity with a volume of 550 A(3) suggesting that the activity of HlyIIR is, modulated by binding of a ligand, which triggers the toxin production., Virtual ligand library screening shows that this pocket can accommodate, compounds with molecular masses of up to 400-500 Da. Based on structural, data and previous biochemical evidence, we propose a model for HlyIIR, interaction with the DNA.
About this Structure
2FX0 is a Single protein structure of sequence from Bacillus cereus. Full crystallographic information is available from OCA.
Reference
Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II., Kovalevskiy OV, Lebedev AA, Surin AK, Solonin AS, Antson AA, J Mol Biol. 2007 Jan 19;365(3):825-34. Epub 2006 Oct 26. PMID:17097673
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