{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Soltysova M"],"funding":["Ministry of Education","European Union - Next Generation EU","European Union","National Institute of virology and bacteriology","Czech Science Foundation","Institute of Organic Chemistry and Biochemistry of the Czech Academy of Sciences"],"pagination":["7305-7320"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11229326"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["52(12)"],"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 understan"],"journal":["Nucleic acids research"],"pubmed_title":["Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function."],"pmcid":["PMC11229326"],"funding_grant_id":["LX22NPO5103","23-06295S"],"pubmed_authors":["Novacek J","Rezacova P","Grishkovskaya I","Skubnik K","Sieglova I","Babiak M","Skerlova J","Pachl P","Krasny L","Soltysova M","Farolfi M","Fabry M"],"additional_accession":[]},"is_claimable":false,"name":"Structural characterization of two prototypical repressors of SorC family reveals tetrameric assemblies on DNA and mechanism of function.","description":"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 understan","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-04-07T16:17:14.463Z","creation":"2025-04-04T11:24:24.351Z"},"accession":"S-EPMC11229326","cross_references":{"pubmed":["38842936"],"doi":["10.1093/nar/gkae434"]}}