4XPU

The crystal structure of EndoV from E.coli

4XPU の概要

• エントリーDOI: 10.2210/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

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

実験手法

X-RAY DIFFRACTION (2.4 Å)