title: Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
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.
authors.affiliation: ESRF, 6 Rue Jules Horowitz, F-38043 Grenoble CEDEX 09, France. muellerd@esrf.fr
authors.forename: Christoph
authors.initials: C
authors.lastname: Mueller-Dieckmann
authors.forename: Stefan
authors.initials: S
authors.lastname: Kernstock
authors.forename: Jochen
authors.initials: J
authors.lastname: Mueller-Dieckmann
authors.forename: Manfred S
authors.initials: MS
authors.lastname: Weiss
authors.forename: Friedrich
authors.initials: F
authors.lastname: Koch-Nolte
mesh_terms: D036002:ADP Ribose Transferases / Q000737:chemistry* / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D001665:Binding Sites; D018360:Crystallography, X-Ray; D006801:Humans; D008274:Magnesium / Q000737:chemistry; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein
chemical_list: D000596:Amino Acids; D036002:ADP Ribose Transferases; D008274:Magnesium