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4XPU

The crystal structure of EndoV from E.coli

4XPU の概要
エントリーDOI10.2210/pdb4xpu/pdb
分子名称Endonuclease V (2 entities in total)
機能のキーワードendonuclease v, inosine, dna repair, rna cleavage, hydrolase
由来する生物種Escherichia coli O45:K1 (strain S88 / ExPEC)
細胞内の位置Cytoplasm : B7MIY4
タンパク質・核酸の鎖数2
化学式量合計47835.39
構造登録者
Xie, W.,Zhang, Z. (登録日: 2015-01-18, 公開日: 2015-08-19, 最終更新日: 2023-11-08)
主引用文献Zhang, Z.,Jia, Q.,Zhou, C.,Xie, W.
Crystal structure of E. coli endonuclease V, an essential enzyme for deamination repair
Sci Rep, 5:12754-12754, 2015
Cited by
PubMed Abstract: Endonuclease V (EndoV) is a ubiquitous protein present in all three kingdoms of life, responsible for the specific cleavages at the second phosphodiester bond 3' to inosine. E. coli EndoV (EcEndoV) is the first member discovered in the EndoV family. It is a small protein with a compact gene organization, yet with a wide spectrum of substrate specificities. However, the structural basis of its substrate recognition is not well understood. In this study, we determined the 2.4 Å crystal structure of EcEndoV. The enzyme preserves the general 'RNase H-like motif' structure. Two subunits are almost fully resolved in the asymmetric unit, but they are not related by any 2-fold axes. Rather, they establish "head-to-shoulder" contacts with loose interactions between each other. Mutational studies show that mutations that disrupt the association mode of the two subunits also decrease the cleavage efficiencies of the enzyme. Further biochemical studies suggest that EcEndoV is able to bind to single-stranded, undamaged DNA substrates without sequence specificity, and forms two types of complexes in a metal-independent manner, which may explain the wide spectrum of substrate specificities of EcEndoV.
PubMed: 26244280
DOI: 10.1038/srep12754
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 4xpu
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2024-10-30に公開中

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