6AMK

Structure of Streptomyces venezuelae BldC-whiI opt complex

Summary for 6AMK

• Entry DOI: 10.2210/pdb6amk/pdb
• Related: 6AMA
• Descriptor: Putative DNA-binding protein, DNA (5'-D(*TP*TP*CP*AP*AP*TP*TP*CP*GP*GP*GP*TP*AP*AP*TP*TP*CP*GP*GP*GP*CP*A)-3'), DNA (5'-D(*AP*AP*TP*GP*TP*CP*CP*GP*AP*AP*TP*TP*AP*CP*CP*CP*GP*AP*AP*TP*TP*G)-3') (3 entities in total)
• Functional Keywords: bldc, streptomyces, merr-like, dna binding protein, dna binding protein-dna complex, dna binding protein/dna
• Biological source: Streptomyces venezuelae; More
• Total number of polymer chains: 4
• Total formula weight: 29841.31

Authors

Schumacher, M.A. (deposition date: 2017-08-09, release date: 2018-03-28, Last modification date: 2024-10-16)

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

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: 29556010
DOI: 10.1038/s41467-018-03576-3

Experimental method

X-RAY DIFFRACTION (3.288 Å)