Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding | Zendy

M. Mietus | Zendy; E. PopowskaNowak | Zendy; Marcin Jaciuk | Zendy; Paweł Kustosz | Zendy; Justyna Studnicka | Zendy; Marcin Nowotny | Zendy

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Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding

Author(s) -

M. Mietus,

E. PopowskaNowak,

Marcin Jaciuk,

Paweł Kustosz,

Justyna Studnicka,

Marcin Nowotny

Publication year - 2014

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gku729

Subject(s) - biology , dna , nuclease , biochemistry , nucleic acid , dna repair , binding site , active site , hydrolase , nucleotide , enzyme , biophysics , gene

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.

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