5N7Y

Solution structure of B. subtilis Sigma G inhibitor CsfB

Summary for 5N7Y

• Entry DOI: 10.2210/pdb5n7y/pdb
• NMR Information: BMRB: 34102
• Descriptor: Anti-sigma-G factor Gin, ZINC ION (2 entities in total)
• Functional Keywords: zinc-finger, dimer, csfb, sigma g inhibitor, transcription
• Biological source: Bacillus subtilis
• Total number of polymer chains: 2
• Total formula weight: 11391.60

Authors

Martinez-Lumbreras, S.,Alfano, C.,Atkinson, A.,Isaacson, R.L. (deposition date: 2017-02-21, release date: 2018-02-28, Last modification date: 2024-06-19)

Primary citation

Martinez-Lumbreras, S.,Alfano, C.,Evans, N.J.,Collins, K.M.,Flanagan, K.A.,Atkinson, R.A.,Krysztofinska, E.M.,Vydyanath, A.,Jackter, J.,Fixon-Owoo, S.,Camp, A.H.,Isaacson, R.L.
Structural and Functional Insights into Bacillus subtilis Sigma Factor Inhibitor, CsfB.
Structure, 26:640-648.e5, 2018

PubMed Abstract: Global changes in bacterial gene expression can be orchestrated by the coordinated activation/deactivation of alternative sigma (σ) factor subunits of RNA polymerase. Sigma factors themselves are regulated in myriad ways, including via anti-sigma factors. Here, we have determined the solution structure of anti-sigma factor CsfB, responsible for inhibition of two alternative sigma factors, σ and σ, during spore formation by Bacillus subtilis. CsfB assembles into a symmetrical homodimer, with each monomer bound to a single Zn ion via a treble-clef zinc finger fold. Directed mutagenesis indicates that dimer formation is critical for CsfB-mediated inhibition of both σ and σ, and we have characterized these interactions in vitro. This work represents an advance in our understanding of how CsfB mediates inhibition of two alternative sigma factors to drive developmental gene expression in a bacterium.

PubMed: 29526435
DOI: 10.1016/j.str.2018.02.007

Experimental method

SOLUTION NMR