5W1E
PobR in complex with PHB
Summary for 5W1E
| Entry DOI | 10.2210/pdb5w1e/pdb |
| Descriptor | Putative transcriptional regulator, SULFATE ION, P-HYDROXYBENZOIC ACID, ... (5 entities in total) |
| Functional Keywords | iclr, transcription factor, transcription |
| Biological source | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
| Total number of polymer chains | 1 |
| Total formula weight | 56042.81 |
| Authors | Page, R.,Peti, W.,Lord, D.M.,Bajaj, R.,Zhang, R. (deposition date: 2017-06-02, release date: 2017-12-13, Last modification date: 2023-10-04) |
| Primary citation | Zhang, R.,Lord, D.M.,Bajaj, R.,Peti, W.,Page, R.,Sello, J.K. A peculiar IclR family transcription factor regulates para-hydroxybenzoate catabolism in Streptomyces coelicolor. Nucleic Acids Res., 46:1501-1512, 2018 Cited by PubMed Abstract: In Streptomyces coelicolor, we identified a para-hydroxybenzoate (PHB) hydroxylase, encoded by gene pobA (SCO3084), which is responsible for conversion of PHB into PCA (protocatechuic acid), a substrate of the β-ketoadipate pathway which yields intermediates of the Krebs cycle. We also found that the transcription of pobA is induced by PHB and is negatively regulated by the product of SCO3209, which we named PobR. The product of this gene is highly unusual in that it is the apparent fusion of two IclR family transcription factors. Bioinformatic analyses, in vivo transcriptional assays, electrophoretic mobility shift assays (EMSAs), DNase I footprinting, and isothermal calorimetry (ITC) were used to elucidate the regulatory mechanism of PobR. We found that PobR loses its high affinity for DNA (i.e., the pobA operator) in the presence of PHB, the inducer of pobA transcription. PHB binds to PobR with a KD of 5.8 μM. Size-exclusion chromatography revealed that PobR is a dimer in the absence of PHB and a monomer in the presence of PHB. The crystal structure of PobR in complex with PHB showed that only one of the two IclR ligand binding domains was occupied, and defined how the N-terminal ligand binding domain engages the effector ligand. PubMed: 29240934DOI: 10.1093/nar/gkx1234 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.06 Å) |
Structure validation
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