2FX0
Crystal Structure of HlyIIR, a Hemolysin II transcriptional Regulator
Summary for 2FX0
| Entry DOI | 10.2210/pdb2fx0/pdb |
| Descriptor | hemolysin II regulatory protein (2 entities in total) |
| Functional Keywords | transcriptional regulator, transcription |
| Biological source | Bacillus cereus |
| Total number of polymer chains | 1 |
| Total formula weight | 23575.23 |
| Authors | Kovalevskiy, O.V.,Lebedev, A.A.,Solonin, A.S.,Antson, A.A. (deposition date: 2006-02-03, release date: 2006-02-21, Last modification date: 2024-11-20) |
| Primary citation | Kovalevskiy, O.V.,Lebedev, A.A.,Surin, A.K.,Solonin, A.S.,Antson, A.A. Crystal Structure of Bacillus cereus HlyIIR, a Transcriptional Regulator of the Gene for Pore-forming Toxin Hemolysin II. J.Mol.Biol., 365:825-834, 2007 Cited by PubMed 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 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. PubMed: 17097673DOI: 10.1016/j.jmb.2006.10.074 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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