1UI5
Crystal structure of gamma-butyrolactone receptor (ArpA like protein)
Summary for 1UI5
| Entry DOI | 10.2210/pdb1ui5/pdb |
| Related | 1UI6 |
| Descriptor | A-factor receptor homolog (2 entities in total) |
| Functional Keywords | helix-turn-helix, alpha-helix-bundle, antibiotic |
| Biological source | Streptomyces coelicolor |
| Total number of polymer chains | 2 |
| Total formula weight | 47813.82 |
| Authors | Natsume, R.,Senda, T.,Horinouchi, S. (deposition date: 2003-07-15, release date: 2004-07-27, Last modification date: 2024-11-13) |
| Primary citation | Natsume, R.,Ohnishi, Y.,Senda, T.,Horinouchi, S. Crystal structure of a gamma-butyrolactone autoregulator receptor protein in Streptomyces coelicolor A3(2) J.Mol.Biol., 336:409-419, 2004 Cited by PubMed Abstract: The gamma-butyrolactone-type autoregulator/receptor systems in the Gram-positive bacterial genus Streptomyces regulate morphological differentiation or antibiotic production, or both. The autoregulator receptors act as DNA-binding proteins, and on binding their cognate ligands (gamma-butyrolactones) they are released from the DNA, thus serving as repressors. The crystal structure of CprB in Streptomyces coelicolor A3(2), a homologue of the A-factor-receptor protein, ArpA, in Streptomyces griseus, was determined. The overall structure of CprB shows that the gamma-butyrolactone receptors belong to the TetR family. CprB is composed of two domains, a DNA-binding domain and a regulatory domain. The regulatory domain contains a hydrophobic cavity, which probably serves as a ligand-binding pocket. On the basis of the crystal structure of CprB and on the analogy of the characteristics of ligand-TetR binding, the binding of gamma-butyrolactones to the regulatory domain of the receptors is supposed to induce the relocation of the DNA-binding domain through conformational changes of residues located between the ligand-binding site and the DNA-binding domain, which would result in the dissociation of the receptors from their target DNA. PubMed: 14757054DOI: 10.1016/j.jmb.2003.12.040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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