7QH5

The crystal structure of the sigma factor SigG1 from Streptomyces tsukubaensis NRRL18488

Summary for 7QH5

• Entry DOI: 10.2210/pdb7qh5/pdb
• Related: 7QH3
• Descriptor: RNA polymerase sigma factor, GLYCEROL (3 entities in total)
• Functional Keywords: sigma factor, streptomyces, transcription, ecf56
• Biological source: Streptomyces tsukubensis NRRL18488
• Total number of polymer chains: 2
• Total formula weight: 80586.66

Authors

Lourenco, F.,Leite, J.P.,Gales, L. (deposition date: 2021-12-10, release date: 2022-12-21, Last modification date: 2023-11-01)

Primary citation

Leite, J.P.,Lourenco, F.,Oliveira, R.,Sousa, S.F.,Mendes, M.V.,Gales, L.
Crystal structures of Streptomyces tsukubaensis sigma factor SigG1 and anti-sigma RsfG.
J.Struct.Biol., 215:108038-108038, 2023

PubMed Abstract: Transcription of specific genes in bacteria under environmental stress is frequently initiated by extracytoplasmic function (ECF) σ factors. ECFs σ factors harbour two conserved domains, σ and σ, for transcription initiation by recognition of the promoter region and recruitment of RNA polymerase (RNAP). The crystal structure of Streptomyces tsukubaensis SigG1, an ECF56-family σ factor, was determined revealing σ, σ and the additional carboxi-terminal domain SnoaL_2 tightly packed in a compact conformation. The structure of anti-sigma RsfG was also determined by X-ray crystallography and shows a rare β-barrel fold. Analysis of the metal binding motifs inside the protein barrel are consistent with Fe(III) binding, which is in agreement with previous findings that the Streptomyces tsukubaensis ECF56 SigG1-RsfG system is involved in metal-ion homeostasis.

PubMed: 37858875
DOI: 10.1016/j.jsb.2023.108038

Experimental method

X-RAY DIFFRACTION (2.2 Å)