4OB4

Structure of the S. venezulae BldD DNA-binding domain

Summary for 4OB4

• Entry DOI: 10.2210/pdb4ob4/pdb
• Related: 2EWT 4OAX 4OAY 4OAZ
• Descriptor: Putative DNA-binding protein (2 entities in total)
• Functional Keywords: bldd dna binding domain, helix turn helix, dna binding protein
• Biological source: Streptomyces coelicolor A3(2)
• Total number of polymer chains: 3
• Total formula weight: 23651.92

Authors

schumacher, M.A.,Tschowri, N.,Buttner, M.,Brennan, R. (deposition date: 2014-01-06, release date: 2014-11-19, Last modification date: 2023-09-20)

Primary citation

Tschowri, N.,Schumacher, M.A.,Schlimpert, S.,Chinnam, N.B.,Findlay, K.C.,Brennan, R.G.,Buttner, M.J.
Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development.
Cell(Cambridge,Mass.), 158:1136-1147, 2014

PubMed Abstract: The cyclic dinucleotide c-di-GMP is a signaling molecule with diverse functions in cellular physiology. Here, we report that c-di-GMP can assemble into a tetramer that mediates the effective dimerization of a transcription factor, BldD, which controls the progression of multicellular differentiation in sporulating actinomycete bacteria. BldD represses expression of sporulation genes during vegetative growth in a manner that depends on c-di-GMP-mediated dimerization. Structural and biochemical analyses show that tetrameric c-di-GMP links two subunits of BldD through their C-terminal domains, which are otherwise separated by ~10 Å and thus cannot effect dimerization directly. Binding of the c-di-GMP tetramer by BldD is selective and requires a bipartite RXD-X8-RXXD signature. The findings indicate a unique mechanism of protein dimerization and the ability of nucleotide signaling molecules to assume alternative oligomeric states to effect different functions.

PubMed: 25171413
DOI: 10.1016/j.cell.2014.07.022

Experimental method

X-RAY DIFFRACTION (2.8 Å)