2024/06/06 by Markéta Šoltysová, Jana Škerlová, Petr Pachl +9 · 1 voice · 1 citation
Biochemistry, Genetics and Molecular Biology · Materials Science · #Bacterial Genetics and Biotechnology #Enzyme Structure and Function #Protein Structure and Dynamics
paper · pdf · doi:10.1093/nar/gkae434
openalex publication_date 2024/06/06 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/22
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.