8R7Y

Deoxyribonucleoside regulator DeoR in complex with the DNA operator

Summary for 8R7Y

• Entry DOI: 10.2210/pdb8r7y/pdb
• Descriptor: Deoxyribonucleoside regulator, OL18 DNA operator, strand 1, OL18 DNA operator, strand 2, ... (4 entities in total)
• Functional Keywords: transcriptional repressor, protein-dna complex, bacillus subtilis, dna binding protein
• Biological source: Bacillus subtilis subsp. subtilis str. 168; More
• Total number of polymer chains: 8
• Total formula weight: 165239.19

Authors

Pachl, P.,Soltysova, M.,Rezacova, P. (deposition date: 2023-11-27, release date: 2024-06-19, Last modification date: 2024-07-17)

Primary citation

Soltysova, M.,Skerlova, J.,Pachl, P.,Skubnik, K.,Fabry, M.,Sieglova, I.,Farolfi, M.,Grishkovskaya, I.,Babiak, M.,Novacek, J.,Krasny, L.,Rezacova, P.
Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function.
Nucleic Acids Res., 52:7305-7320, 2024

PubMed Abstract: The SorC family of transcriptional regulators plays a crucial role in controlling the carbohydrate metabolism and quorum sensing. We employed an integrative approach combining X-ray crystallography and cryo-electron microscopy to investigate architecture and functional mechanism of two prototypical representatives of two sub-classes of the SorC family: DeoR and CggR from Bacillus subtilis. Despite possessing distinct DNA-binding domains, both proteins form similar tetrameric assemblies when bound to their respective DNA operators. Structural analysis elucidates the process by which the CggR-regulated gapA operon is derepressed through the action of two effectors: fructose-1,6-bisphosphate and newly confirmed dihydroxyacetone phosphate. Our findings provide the first comprehensive understanding of the DNA binding mechanism of the SorC-family proteins, shedding new light on their functional characteristics.

PubMed: 38842936
DOI: 10.1093/nar/gkae434

Experimental method

X-RAY DIFFRACTION (3.7 Å)