3W0F

Crystal structure of mouse Endonuclease VIII-LIKE 3 (mNEIL3)

3W0F の概要

• エントリーDOI: 10.2210/pdb3w0f/pdb
• 分子名称: Endonuclease 8-like 3, ZINC ION, IODIDE ION, ... (4 entities in total)
• 機能のキーワード: helix two turns helix, zinc finger, dna binding, hydrolase
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Nucleus: Q8K203
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 32420.91

構造登録者

Liu, M.,Imamura, K.,Averill, A.M.,Wallace, S.S.,Doublie, S. (登録日: 2012-10-30, 公開日: 2013-01-16, 最終更新日: 2024-03-20)

主引用文献

Liu, M.,Imamura, K.,Averill, A.M.,Wallace, S.S.,Doublie, S.
Structural Characterization of a Mouse Ortholog of Human NEIL3 with a Marked Preference for Single-Stranded DNA
Structure, 21:247-256, 2013

PubMed Abstract: Endonuclease VIII-like 3 (Neil3) is a DNA glycosylase of the base excision repair pathway that protects cells from oxidative DNA damage by excising a broad spectrum of cytotoxic and mutagenic base lesions. Interestingly, Neil3 exhibits an unusual preference for DNA with single-stranded regions. Here, we report the 2.0 Å crystal structure of a Neil3 enzyme. Although the glycosylase region of mouse Neil3 (MmuNeil3Δ324) exhibits the same overall fold as that of other Fpg/Nei proteins, it presents distinct structural features. First, MmuNeil3Δ324 lacks the αF-β9/10 loop that caps the flipped-out 8-oxoG in bacterial Fpg, which is consistent with its inability to cleave 8-oxoguanine. Second, Neil3 not only lacks two of the three void-filling residues that stabilize the opposite strand, but it also harbors negatively charged residues that create an unfavorable electrostatic environment for the phosphate backbone of that strand. These structural features provide insight into the substrate specificity and marked preference of Neil3 for ssDNA.

PubMed: 23313161
DOI: 10.1016/j.str.2012.12.008

実験手法

X-RAY DIFFRACTION (2 Å)