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spinqualitylabelsall models ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, 1khz Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function ADP-ribose pyrophosphatase (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. ADPRP regulates the level of ADP-ribose (ADPR) in the cell. Excess of ADPR can inactivate proteins with nucleotide-binding site by binding to them.[1] Structural highlights ADPRP contains two domains: the and the C-terminal which contains the active site. The C-terminal domain contains the which is typical to pyrophosphatases and binds the metal ion. .[2]

3D structures of ADP-ribose pyrophosphatase

Updated on 01-November-2016 {{#tree:id=OrganizedByTopic|openlevels=0|

• ADP-ribose pyrophosphatase

• • 1q33 – hADPRP NUDT9 residues 59-350 – human
    
  • 1v8i, 3x0i, 3x0j - TtADPRP – Thermus thermophilus
    
  • 3x0k, 3k0l - TtADPRP ES-state
    
  • 3x0m, 3k0n - TtADPRP ESM-state
    
  • 3x0o, [[3k0p], 3k0q] - TtADPRP ESMM-state
    
  • 3x0r, 3k0s - TtADPRP E'-state
    
  • 2w4e – ADPRP residues 56-200 – Deinococcus radiodurans
    
  • 3o8s - ADPRP – Streptococcus suis
    
  • 4kyx – ADPRP Mutt – Rickettsia felis
    
  • 5i8u - ADPRP – Mycobacterium tuberculosis
    

• ADP-ribose pyrophosphatase binary complex

• • 1v8l – TtADPRP + ADPR
    
  • 1v8n - TtADPRP + Zn
    

• ADP-ribose pyrophosphatase ternary complex

• • 1khz - EcADPRP + AMPCPR + Mg – Escherichia coli
    
  • 1qvj - hADPRP + ribose-5-phosphate + Mg
    
  • 1v8m - TtADPRP + Gd + ADPR
    
  • 1v8s - TtADPRP + AMP + Mg
    
  • 1v8t - TtADPRP + ribose-5-phosphate + Zn
    
  • 1v8u - TtADPRP (mutant) + sulfate + Mg
    
  • 1v8v - TtADPRP (mutant) + ADPR + Mg
    
  • 1v8w - TtADPRP (mutant) + sulfate + Zn
    
  • 1v8y - TtADPRP (mutant) + ADPR + Zn
    
  • 1v8r - TtADPRP + ADPR + Zn
    
  • 3bm4 - hADPRP NUDT5 + AMPCPR + Mg
    

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References

1. ↑ 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
2. ↑ Gabelli SB, Bianchet MA, Ohnishi Y, Ichikawa Y, Bessman MJ, Amzel LM. Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase. Biochemistry. 2002 Jul 30;41(30):9279-85. PMID:12135348