| http://purl.uniprot.org/citations/27580719 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27580719 | http://www.w3.org/2000/01/rdf-schema#comment | "Thymine DNA Glycosylase (TDG) is a base excision repair enzyme functioning in DNA repair and epigenetic regulation. TDG removes thymine from mutagenic G·T mispairs arising from deamination of 5-methylcytosine (mC), and it processes other deamination-derived lesions including uracil (U). Essential for DNA demethylation, TDG excises 5-formylcytosine and 5-carboxylcytosine, derivatives of mC generated by Tet (ten-eleven translocation) enzymes. Here, we report structural and functional studies of TDG82-308, a new construct containing 29 more N-terminal residues than TDG111-308, the construct used for previous structures of DNA-bound TDG. Crystal structures and NMR experiments demonstrate that most of these N-terminal residues are disordered, for substrate- or product-bound TDG82-308 Nevertheless, G·T substrate affinity and glycosylase activity of TDG82-308 greatly exceeds that of TDG111-308 and is equivalent to full-length TDG. We report the first high-resolution structures of TDG in an enzyme-substrate complex, for G·U bound to TDG82-308 (1.54 Å) and TDG111-308 (1.71 Å), revealing new enzyme-substrate contacts, direct and water-mediated. We also report a structure of the TDG82-308 product complex (1.70 Å). TDG82-308 forms unique enzyme-DNA interactions, supporting its value for structure-function studies. The results advance understanding of how TDG recognizes and removes modified bases from DNA, particularly those resulting from deamination."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.org/dc/terms/identifier | "doi:10.1093/nar/gkw768"xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/author | "Drohat A.C."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/author | "Pozharski E."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/author | "Pidugu L.S."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/author | "Varney K.M."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/author | "Malik S.S."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/author | "Coey C.T."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/name | "Nucleic Acids Res"xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/pages | "10248-10258"xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/title | "Structural basis of damage recognition by thymine DNA glycosylase: Key roles for N-terminal residues."xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://purl.uniprot.org/core/volume | "44"xsd:string |
| http://purl.uniprot.org/citations/27580719 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27580719 |
| http://purl.uniprot.org/citations/27580719 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/27580719 |
| http://purl.uniprot.org/uniprot/#_Q13569-mappedCitation-27580719 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/27580719 |
| http://purl.uniprot.org/uniprot/Q13569 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/27580719 |