ADP-ribose pyrophosphatase
From Proteopedia
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== Structural highlights == | == 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/7'>Nudix (Nucleoside Diphosphate linked to X) sequence</scene> which is typical to pyrophosphatases and binds the metal ion. <scene name='48/488514/Cv/ | + | 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/8'>Residues from both monomers of ADPRP participate in the active site</scene>. |
</StructureSection> | </StructureSection> | ||
==3D structures of ADP-ribose pyrophosphatase== | ==3D structures of ADP-ribose pyrophosphatase== | ||
Revision as of 11:41, 6 December 2015
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3D structures of ADP-ribose pyrophosphatase
Updated on 06-December-2015
References
- ↑ 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
