2Q24
Crystal structure of TetR transcriptional regulator SCO0520 from Streptomyces coelicolor
Summary for 2Q24
| Entry DOI | 10.2210/pdb2q24/pdb |
| Descriptor | Putative tetR family transcriptional regulator, ACETATE ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | transcriptional regulator, structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, transcription |
| Biological source | Streptomyces coelicolor A3(2) |
| Total number of polymer chains | 2 |
| Total formula weight | 42209.03 |
| Authors | Cymborowski, M.,Chruszcz, M.,Koclega, K.D.,Filippova, E.V.,Xu, X.,Gu, J.,Savchenko, A.,Edwards, A.M.,Joachimiak, A.,Minor, W.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2007-05-25, release date: 2007-07-03, Last modification date: 2024-11-20) |
| Primary citation | Filippova, E.V.,Chruszcz, M.,Cymborowski, M.,Gu, J.,Savchenko, A.,Edwards, A.,Minor, W. Crystal structure of a putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) reveals an unusual dimer among TetR family proteins. J.Struct.Funct.Genom., 12:149-157, 2011 Cited by PubMed Abstract: A structure of the apo-form of the putative transcriptional regulator SCO0520 from Streptomyces coelicolor A3(2) was determined at 1.8 Å resolution. SCO0520 belongs to the TetR family of regulators. In the crystal lattice, the asymmetric unit contains two monomers that form an Ω-shaped dimer. The distance between the two DNA-recognition domains is much longer than the corresponding distances in the known structures of other TetR family proteins. In addition, the subunits in the dimer have different conformational states, resulting in different relative positions of the DNA-binding and regulatory domains. Similar conformational modifications are observed in other TetR regulators and result from ligand binding. These studies provide information about the flexibility of SCO0520 molecule and its putative biological function. PubMed: 21625866DOI: 10.1007/s10969-011-9112-4 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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