4Q0W

he catalytic core of Rad2 in complex with DNA substrate (complex II)

Summary for 4Q0W

• Entry DOI: 10.2210/pdb4q0w/pdb
• Related: 4Q0R 4Q0Z 4Q10
• Descriptor: DNA repair protein RAD2, DNA (5'-D(*TP*TP*TP*GP*AP*TP*CP*CP*GP*TP*CP*CP*AP*CP*CP*TP*TP*T)-3'), DNA (5'-D(*TP*TP*AP*GP*GP*TP*GP*GP*AP*CP*GP*GP*AP*TP*CP*AP*TP*T)-3'), ... (6 entities in total)
• Functional Keywords: ba rossmann-like, dna repair, tfiih, nucleus, hydrolase-dna complex, hydrolase/dna
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus: P07276
• Total number of polymer chains: 4
• Total formula weight: 95531.60

Authors

Mietus, M.,Nowak, E.,Jaciuk, M.,Kustosz, P.,Nowotny, M. (deposition date: 2014-04-02, release date: 2014-08-27, Last modification date: 2023-09-20)

Primary citation

Mietus, M.,Nowak, E.,Jaciuk, M.,Kustosz, P.,Studnicka, J.,Nowotny, M.
Crystal structure of the catalytic core of Rad2: insights into the mechanism of substrate binding.
Nucleic Acids Res., 42:10762-10775, 2014

PubMed 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.

PubMed: 25120270
DOI: 10.1093/nar/gku729

Experimental method

X-RAY DIFFRACTION (2.1 Å)