2b18
From Proteopedia
(New page: 200px<br /><applet load="2b18" size="450" color="white" frame="true" align="right" spinBox="true" caption="2b18, resolution 1.80Å" /> '''N-terminal GAF domai...) |
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| - | [[Image:2b18.gif|left|200px]]<br /><applet load="2b18" size=" | + | [[Image:2b18.gif|left|200px]]<br /><applet load="2b18" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2b18, resolution 1.80Å" /> | caption="2b18, resolution 1.80Å" /> | ||
'''N-terminal GAF domain of transcriptional pleiotropic repressor CodY.'''<br /> | '''N-terminal GAF domain of transcriptional pleiotropic repressor CodY.'''<br /> | ||
==Overview== | ==Overview== | ||
| - | CodY is a global regulator of transcription in gram-positive bacteria. It | + | CodY is a global regulator of transcription in gram-positive bacteria. It represses during growth genes required for adaptation to nutrient limitation, including virulence genes in some human pathogens. CodY activity is regulated by GTP and branched chain amino acids, metabolites whose intracellular concentrations drop as cells enter stationary phase. Although CodY has a highly conserved sequence, it has no significant similarity to proteins of known structure. Here we report crystal structures of two fragments of CodY from Bacillus subtilis that clearly constitute its cofactor and DNA binding domains and reveal that CodY is a chimera of previously observed folding units. The N-terminal cofactor-binding fragment adopts a fold reminiscent of the GAF domains found in cyclic nucleotide phosphodiesterases and adenylate cyclases. It is a dimer stabilized by an intermolecular six alpha-helical bundle that buries an extensive apolar surface rich in residues invariant in CodY orthologues. The branched chain amino acid ligands reside in hydrophobic pockets of each monomer distal to the dimer-forming surface. The structure of the C-terminal DNA binding domain belongs to the winged helix-turn-helix family. The implications of the structure for DNA binding by CodY and its control by cofactor binding are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 2B18 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with ILE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2B18 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=ILE:'>ILE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B18 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Blagova, E.]] | [[Category: Blagova, E.]] | ||
[[Category: Joseph, P.]] | [[Category: Joseph, P.]] | ||
| - | [[Category: Levdikov, V | + | [[Category: Levdikov, V M.]] |
| - | [[Category: Sonenshein, A | + | [[Category: Sonenshein, A L.]] |
| - | [[Category: Wilkinson, A | + | [[Category: Wilkinson, A J.]] |
[[Category: ILE]] | [[Category: ILE]] | ||
[[Category: cody]] | [[Category: cody]] | ||
[[Category: dna-binding; nucleotide-binding; repressor; transcription regulation; gaf domain; branched chain amino acid binding.]] | [[Category: dna-binding; nucleotide-binding; repressor; transcription regulation; gaf domain; branched chain amino acid binding.]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:33:05 2008'' |
Revision as of 14:33, 21 February 2008
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N-terminal GAF domain of transcriptional pleiotropic repressor CodY.
Overview
CodY is a global regulator of transcription in gram-positive bacteria. It represses during growth genes required for adaptation to nutrient limitation, including virulence genes in some human pathogens. CodY activity is regulated by GTP and branched chain amino acids, metabolites whose intracellular concentrations drop as cells enter stationary phase. Although CodY has a highly conserved sequence, it has no significant similarity to proteins of known structure. Here we report crystal structures of two fragments of CodY from Bacillus subtilis that clearly constitute its cofactor and DNA binding domains and reveal that CodY is a chimera of previously observed folding units. The N-terminal cofactor-binding fragment adopts a fold reminiscent of the GAF domains found in cyclic nucleotide phosphodiesterases and adenylate cyclases. It is a dimer stabilized by an intermolecular six alpha-helical bundle that buries an extensive apolar surface rich in residues invariant in CodY orthologues. The branched chain amino acid ligands reside in hydrophobic pockets of each monomer distal to the dimer-forming surface. The structure of the C-terminal DNA binding domain belongs to the winged helix-turn-helix family. The implications of the structure for DNA binding by CodY and its control by cofactor binding are discussed.
About this Structure
2B18 is a Single protein structure of sequence from Bacillus subtilis with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of CodY, a GTP- and isoleucine-responsive regulator of stationary phase and virulence in gram-positive bacteria., Levdikov VM, Blagova E, Joseph P, Sonenshein AL, Wilkinson AJ, J Biol Chem. 2006 Apr 21;281(16):11366-73. Epub 2006 Feb 17. PMID:16488888
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