ADP-ribose pyrophosphatase

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Revision as of 11:40, 6 December 2015

ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, 1khz

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Updated on 06-December-2015

↑ Gabelli SB, Bianchet MA, Bessman MJ, Amzel LM. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family. Nat Struct Biol. 2001 May;8(5):467-72. PMID:11323725 doi:10.1038/87647

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 == Structural highlights ==
-ADPRP contains two domains: the <scene name='48/488514/Cv/6'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site.  The C-terminal domain contains the <scene name='48/488514/Cv/3'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/5'>Residues from both monomers of ADPRP participate in the active site</scene>.
+ADPRP contains two domains: the <scene name='48/488514/Cv/6'>N-terminal domain responsible for dimer stabilization</scene> and the C-terminal which contains the active site.  The C-terminal domain contains the <scene name='48/488514/Cv/7'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/5'>Residues from both monomers of ADPRP participate in the active site</scene>.
 </StructureSection>
 ==3D structures of ADP-ribose pyrophosphatase==