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 2.40&Aring;" /> '''Crystal Structure of...)
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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Antson, A.A.]]
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[[Category: Antson, A A.]]
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[[Category: Kovalevskiy, O.V.]]
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[[Category: Kovalevskiy, O V.]]
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[[Category: Lebedev, A.A.]]
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[[Category: Lebedev, A A.]]
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[[Category: Solonin, A.S.]]
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[[Category: Solonin, A S.]]
[[Category: transcriptional regulator]]
[[Category: transcriptional regulator]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 19:46:38 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:25:57 2008''

Revision as of 15:26, 21 February 2008


2fx0, resolution 2.40Å

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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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