2QTY

Crystal Structure of mouse ADP-ribosylhydrolase 3 (mARH3)

2QTY の概要

• エントリーDOI: 10.2210/pdb2qty/pdb
• 分子名称: Poly(ADP-ribose) glycohydrolase ARH3, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: hydrolase, adp-ribose, magnesium, metal-binding, nucleus
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Cytoplasm: Q8CG72
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75337.42

構造登録者

Mueller-Dieckmann, C. (登録日: 2007-08-03, 公開日: 2008-03-04, 最終更新日: 2023-08-30)

主引用文献

Mueller-Dieckmann, C.,Kernstock, S.,Mueller-Dieckmann, J.,Weiss, M.S.,Koch-Nolte, F.
Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
Acta Crystallogr.,Sect.F, 64:156-162, 2008

PubMed Abstract: ADP-ribosylation is a reversible and covalent post-translational modification in which the attachment of ADP-ribose is catalyzed by ADP-ribosyltransferases and the removal of ADP-ribose is catalyzed by ADP-ribosylhydrolases. ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. The three-dimensional structure has been resolved at a resolution of 1.8 A. The structure constitutes a compact all-alpha-helical protein with two Mg(2+) ions located in the active-site crevice. A structural comparison of mouse ADP-ribosylhydrolase 3 with its human orthologue shows a high degree of structural similarity. Furthermore, four prokaryotic proteins deposited in the PDB could be identified as being structurally related.

PubMed: 18323597
DOI: 10.1107/S1744309108001413

実験手法

X-RAY DIFFRACTION (1.8 Å)