2QTY

Crystal Structure of mouse ADP-ribosylhydrolase 3 (mARH3)

Summary for 2QTY

• Entry DOI: 10.2210/pdb2qty/pdb
• Descriptor: Poly(ADP-ribose) glycohydrolase ARH3, MAGNESIUM ION (3 entities in total)
• Functional Keywords: hydrolase, adp-ribose, magnesium, metal-binding, nucleus
• Biological source: Mus musculus (house mouse)
• Cellular location: Cytoplasm: Q8CG72
• Total number of polymer chains: 2
• Total formula weight: 75337.42

Authors

Mueller-Dieckmann, C. (deposition date: 2007-08-03, release date: 2008-03-04, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)