Abstract:
:Rad2/XPG belongs to the flap nuclease family and is responsible for a key step of the eukaryotic nucleotide excision DNA repair (NER) pathway. To elucidate the mechanism of DNA binding by Rad2/XPG, we solved crystal structures of the catalytic core of Rad2 in complex with a substrate. Rad2 utilizes three structural modules for recognition of the double-stranded portion of DNA substrate, particularly a Rad2-specific α-helix for binding the cleaved strand. The protein does not specifically recognize the single-stranded portion of the nucleic acid. Our data suggest that in contrast to related enzymes (FEN1 and EXO1), the Rad2 active site may be more accessible, which would create an exit route for substrates without a free 5' end.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Miętus M,Nowak E,Jaciuk M,Kustosz P,Studnicka J,Nowotny Mdoi
10.1093/nar/gku729subject
Has Abstractpub_date
2014-01-01 00:00:00pages
10762-75issue
16eissn
0305-1048issn
1362-4962pii
gku729journal_volume
42pub_type
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