{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Muller AU"],"funding":["Swiss National Science Foundation"],"pagination":["4653"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6789036"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(1)"],"pubmed_abstract":["In mycobacteria, transcriptional activator PafBC is responsible for upregulating the majority of genes induced by DNA damage. Understanding the mechanism of PafBC activation is impeded by a lack of structural information on this transcription factor that contains a widespread, but poorly understood WYL domain frequently encountered in bacterial transcription factors. Here, we determine the crystal structure of Arthrobacter aurescens PafBC. The protein consists of two modules, each harboring an N-terminal helix-turn-helix DNA-binding domain followed by a central WYL and a C-terminal extension (WCX) domain. The WYL domains exhibit Sm-folds, while the WCX domains adopt ferredoxin-like folds, both characteristic for RNA-binding proteins. Our results suggest a mechanism of regulation in which W"],"journal":["Nature communications"],"pubmed_title":["Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC."],"pmcid":["PMC6789036"],"funding_grant_id":["163314","31003A-163314"],"pubmed_authors":["Muller AU","Ban N","Weber-Ban E","Leibundgut M"],"additional_accession":[]},"is_claimable":false,"name":"Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC.","description":"In mycobacteria, transcriptional activator PafBC is responsible for upregulating the majority of genes induced by DNA damage. Understanding the mechanism of PafBC activation is impeded by a lack of structural information on this transcription factor that contains a widespread, but poorly understood WYL domain frequently encountered in bacterial transcription factors. Here, we determine the crystal structure of Arthrobacter aurescens PafBC. The protein consists of two modules, each harboring an N-terminal helix-turn-helix DNA-binding domain followed by a central WYL and a C-terminal extension (WCX) domain. The WYL domains exhibit Sm-folds, while the WCX domains adopt ferredoxin-like folds, both characteristic for RNA-binding proteins. Our results suggest a mechanism of regulation in which W","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Oct","modification":"2026-04-15T21:22:07.867Z","creation":"2019-10-19T07:22:10Z"},"accession":"S-EPMC6789036","cross_references":{"pubmed":["31604936"],"doi":["10.1038/s41467-019-12567-x"]}}