Structure of mouse ADP-ribosylhydrolase 3 (mARH3)

نویسندگان

  • Christoph Mueller-Dieckmann
  • Stefan Kernstock
  • Jochen Mueller-Dieckmann
  • Manfred S. Weiss
  • Friedrich Koch-Nolte
چکیده

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.

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عنوان ژورنال:
  • Acta Crystallographica Section F: Structural Biology and Crystallization Communications

دوره 64  شماره 

صفحات  -

تاریخ انتشار 2008