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Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function
Nucleic Acids Research 2024: Early View
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.
Foldamers controlled by functional triamino acids: structural investigation of α/γ-hybrid oligopeptides
Communications Chemistry 7: 114 (2024)
Ab Initio Calculation of UV–vis Absorption of Parent Mg, Fe, Co, Ni, Cu, and Zn Metalloporphyrins
Inorganic Chemistry 63 (22): 10127–10142 (2024)
Design Rules for the Nano-Bio Interface of Nanodiamonds: Implications for siRNA Vectorization
Advanced Functional Materials 2024: Early View