Structure of mouse ADP-ribosylhydrolase 3 (mARH3).
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.
Mueller-Dieckmann
Christoph
C
ESRF, 6 Rue Jules Horowitz, F-38043 Grenoble CEDEX 09, France. muellerd@esrf.fr
Kernstock
Stefan
S
Mueller-Dieckmann
Jochen
J
Weiss
Manfred S
MS
Koch-Nolte
Friedrich
F
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
D000596:Amino Acids; D036002:ADP Ribose Transferases; D008274:Magnesium