{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wu S"],"funding":["Natural Science Foundation of Guangdong Province (Guangdong Natural Science Foundation)","National Natural Science Foundation of China (National Science Foundation of China)"],"pagination":["8861"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12501005"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["16(1)"],"pubmed_abstract":["The ability of transcription factors to recognize diverse DNA sequences while maintaining binding specificity is required for gene regulation, but the molecular mechanism enabling this flexibility remains poorly understood. Here, we show that the DNA-binding domain of transcription factor AflR employs a structured zinc cluster motif and disordered terminal regions to achieve sequence-diverse DNA recognition. Using NMR spectroscopy, molecular dynamics simulations, and biochemical approaches, we demonstrate that the DNA-binding domain of AflR contains a structured zinc cluster core flanked by dynamic terminal regions. Two AflR DNA-binding domain monomers recognize inverted CG half-sites, with the zinc cluster motif providing sequence-specific anchoring while dynamic termini optimize binding "],"journal":["Nature communications"],"pubmed_title":["Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR."],"pmcid":["PMC12501005"],"funding_grant_id":["2021TQ06N115","22307022","2024A1515010062"],"pubmed_authors":["Zhang W","Huang S","Liu Z","Fernie AR","Zhang X","Wu S","Wang F","Zhou W","Wang W","Yan S","Zhan L"],"additional_accession":[]},"is_claimable":false,"name":"Conformational plasticity of disordered regions enables sequence-diverse DNA recognition by transcription factor AflR.","description":"The ability of transcription factors to recognize diverse DNA sequences while maintaining binding specificity is required for gene regulation, but the molecular mechanism enabling this flexibility remains poorly understood. Here, we show that the DNA-binding domain of transcription factor AflR employs a structured zinc cluster motif and disordered terminal regions to achieve sequence-diverse DNA recognition. Using NMR spectroscopy, molecular dynamics simulations, and biochemical approaches, we demonstrate that the DNA-binding domain of AflR contains a structured zinc cluster core flanked by dynamic terminal regions. Two AflR DNA-binding domain monomers recognize inverted CG half-sites, with the zinc cluster motif providing sequence-specific anchoring while dynamic termini optimize binding ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Oct","modification":"2026-06-04T06:21:11.59Z","creation":"2026-05-06T03:12:34.756Z"},"accession":"S-EPMC12501005","cross_references":{"pubmed":["41053219"],"doi":["10.1038/s41467-025-63926-w"]}}