<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Muller AU</submitter><funding>Swiss National Science Foundation</funding><pagination>4653</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6789036</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>10(1)</volume><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</pubmed_abstract><journal>Nature communications</journal><pubmed_title>Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC.</pubmed_title><pmcid>PMC6789036</pmcid><funding_grant_id>163314</funding_grant_id><funding_grant_id>31003A-163314</funding_grant_id><pubmed_authors>Muller AU</pubmed_authors><pubmed_authors>Ban N</pubmed_authors><pubmed_authors>Weber-Ban E</pubmed_authors><pubmed_authors>Leibundgut M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC.</name><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</description><dates><release>2019-01-01T00:00:00Z</release><publication>2019 Oct</publication><modification>2026-04-15T21:22:07.867Z</modification><creation>2019-10-19T07:22:10Z</creation></dates><accession>S-EPMC6789036</accession><cross_references><pubmed>31604936</pubmed><doi>10.1038/s41467-019-12567-x</doi></cross_references></HashMap>