6PFV

Structure of S. venezuelae RisG-WhiG-c-di-GMP complex: orthorhombic crystal form

Summary for 6PFV

• Entry DOI: 10.2210/pdb6pfv/pdb
• Related: 6PFJ
• Descriptor: AmfC protein, RNA polymerase sigma factor, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) (3 entities in total)
• Functional Keywords: rsig, whig, c-di-gmp, sigma, anti-sigma, streptomyces, transcription
• Biological source: Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD 04745); More
• Total number of polymer chains: 6
• Total formula weight: 156549.14

Authors

Schumacher, M.A. (deposition date: 2019-06-22, release date: 2019-11-13, Last modification date: 2023-10-11)

Primary citation

Gallagher, K.A.,Schumacher, M.A.,Bush, M.J.,Bibb, M.J.,Chandra, G.,Holmes, N.A.,Zeng, W.,Henderson, M.,Zhang, H.,Findlay, K.C.,Brennan, R.G.,Buttner, M.J.
c-di-GMP Arms an Anti-sigma to Control Progression of Multicellular Differentiation in Streptomyces.
Mol.Cell, 77:586-, 2020

PubMed Abstract: Streptomyces are our primary source of antibiotics, produced concomitantly with the transition from vegetative growth to sporulation in a complex developmental life cycle. We previously showed that the signaling molecule c-di-GMP binds BldD, a master repressor, to control initiation of development. Here we demonstrate that c-di-GMP also intervenes later in development to control differentiation of the reproductive hyphae into spores by arming a novel anti-σ (RsiG) to bind and sequester a sporulation-specific σ factor (σ). We present the structure of the RsiG-(c-di-GMP)-σ complex, revealing an unusual, partially intercalated c-di-GMP dimer bound at the RsiG-σ interface. RsiG binds c-di-GMP in the absence of σ, employing a novel E(X)S(X)R(X)Q(X)D motif repeated on each helix of a coiled coil. Further studies demonstrate that c-di-GMP is essential for RsiG to inhibit σ. These findings reveal a newly described control mechanism for σ-anti-σ complex formation and establish c-di-GMP as the central integrator of Streptomyces development.

PubMed: 31810759
DOI: 10.1016/j.molcel.2019.11.006

Experimental method

X-RAY DIFFRACTION (3 Å)