6AMA
Structure of S. coelicolor/S. venezuelae BldC-smeA-ssfA complex to 3.09 Angstrom
Summary for 6AMA
| Entry DOI | 10.2210/pdb6ama/pdb |
| Descriptor | Putative DNA-binding protein, DNA (99-MER) (3 entities in total) |
| Functional Keywords | bldc, s. coelicolor, developmental switch, merr-like, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Streptomyces venezuelae More |
| Total number of polymer chains | 13 |
| Total formula weight | 147327.10 |
| Authors | Schumacher, M.A. (deposition date: 2017-08-09, release date: 2018-03-28, Last modification date: 2023-10-04) |
| Primary citation | Schumacher, M.A.,den Hengst, C.D.,Bush, M.J.,Le, T.B.K.,Tran, N.T.,Chandra, G.,Zeng, W.,Travis, B.,Brennan, R.G.,Buttner, M.J. The MerR-like protein BldC binds DNA direct repeats as cooperative multimers to regulate Streptomyces development. Nat Commun, 9:1139-1139, 2018 Cited by PubMed Abstract: Streptomycetes are notable for their complex life cycle and production of most clinically important antibiotics. A key factor that controls entry into development and the onset of antibiotic production is the 68-residue protein, BldC. BldC is a putative DNA-binding protein related to MerR regulators, but lacks coiled-coil dimerization and effector-binding domains characteristic of classical MerR proteins. Hence, the molecular function of the protein has been unclear. Here we show that BldC is indeed a DNA-binding protein and controls a regulon that includes other key developmental regulators. Intriguingly, BldC DNA-binding sites vary significantly in length. Our BldC-DNA structures explain this DNA-binding capability by revealing that BldC utilizes a DNA-binding mode distinct from MerR and other known regulators, involving asymmetric head-to-tail oligomerization on DNA direct repeats that results in dramatic DNA distortion. Notably, BldC-like proteins radiate throughout eubacteria, establishing BldC as the founding member of a new structural family of regulators. PubMed: 29556010DOI: 10.1038/s41467-018-03576-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.09 Å) |
Structure validation
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