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

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 Res

journal_title

Nucleic acids research

authors

Miętus M,Nowak E,Jaciuk M,Kustosz P,Studnicka J,Nowotny M

doi

10.1093/nar/gku729

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

10762-75

issue

16

eissn

0305-1048

issn

1362-4962

pii

gku729

journal_volume

42

pub_type

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