2HGV
N-terminal GAF domain of transcriptional pleiotropic repressor CodY
Summary for 2HGV
| Entry DOI | 10.2210/pdb2hgv/pdb |
| Related | 2B0L 2B18 2GX5 |
| Descriptor | GTP-sensing transcriptional pleiotropic repressor codY, VALINE (3 entities in total) |
| Functional Keywords | cody, dna-binding, nucleotide-binding, repressor, transcription regulation, gaf domain, branched chain amino acid binding, dna binding protein |
| Biological source | Bacillus subtilis |
| Cellular location | Cytoplasm: P39779 |
| Total number of polymer chains | 1 |
| Total formula weight | 18948.54 |
| Authors | Wilkinson, A.J.,Levdikov, V.M.,Blagova, E.V. (deposition date: 2006-06-27, release date: 2006-08-15, Last modification date: 2023-11-15) |
| Primary citation | Levdikov, V.M.,Blagova, E.,Joseph, P.,Sonenshein, A.L.,Wilkinson, A.J. The Structure of CodY, a GTP- and Isoleucine-responsive Regulator of Stationary Phase and Virulence in Gram-positive Bacteria J.Biol.Chem., 281:11366-11373, 2006 Cited by PubMed Abstract: 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. PubMed: 16488888DOI: 10.1074/jbc.M513015200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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