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Crystal structure of Bacillus cereus HlyIIR, a transcriptional regulator of the gene for pore-forming toxin hemolysin II

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JournalJournal of Molecular Biology
DatePublished - 19 Jan 2007
Issue number3
Volume365
Number of pages10
Pages (from-to)825-834
Original languageEnglish

Abstract

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 angstrom(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. (c) 2006 Elsevier Ltd. All rights reserved.

    Research areas

  • HlyIIR, X-ray crystallography, DNA-binding, TetR family, hemolysin II, MOLECULAR-GRAPHICS, BINDING PROTEIN, TET REPRESSOR, DNA-BINDING, SEQUENCE, RESISTANCE, REFINEMENT, VIRULENCE, ANTHRACIS, RECEPTOR

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