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4Q10

The catalytic core of Rad2 in complex with DNA substrate (complex IV)

4Q10 の概要
エントリーDOI10.2210/pdb4q10/pdb
関連するPDBエントリー4Q0W 4Q0Z 4Q10
分子名称DNA repair protein RAD2, DNA (5'-D(*TP*TP*TP*TP*GP*CP*TP*CP*CP*CP*TP*TP*GP*TP*CP*TP*CP*AP*GP*TP*TP*TP*T)-3'), DNA (5'-D(*TP*TP*TP*TP*CP*TP*GP*AP*GP*AP*CP*AP*AP*GP*GP*GP*AP*GP*CP*TP*TP*TP*T)-3'), ... (6 entities in total)
機能のキーワードba rossmann-like, dna repair, tfiih, nucleus, hydrolase-dna complex, hydrolase/dna
由来する生物種Saccharomyces cerevisiae (Baker's yeast)
詳細
細胞内の位置Nucleus: P07276
タンパク質・核酸の鎖数4
化学式量合計98583.53
構造登録者
Mietus, M.,Nowak, E.,Jaciuk, M.,Kustosz, P.,Nowotny, M. (登録日: 2014-04-02, 公開日: 2014-08-27, 最終更新日: 2023-09-20)
主引用文献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
Cited by
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
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.7 Å)
構造検証レポート
Validation report summary of 4q10
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-11-13に公開中

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