ADP-ribose pyrophosphatase

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{{STRUCTURE_1v8v| PDB=1v8v | SIZE=400| SCENE= |right|CAPTION=ADP-ribose pyrophosphatase complex with ADP-ribose and Mg+2 ion, [[1v8v]] }}
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Revision as of 08:04, 3 April 2012

Template:STRUCTURE 1v8v

ADP-ribose pyrophosphatase (ADPRP) catalyzes the reaction which converts ADP-ribose to AMP and D-ribose 5-phosphate. ADPRP contains Mg+2 ion. The C terminal of ADPRP contains the Nudix sequence which binds the metal 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.

3D structures of ADP-ribose pyrophosphatase

1q33 – hADPRP NUDT9 residues 59-350 – human
1v8i - TtADPRP – Thermus thermophilus
2w4e– ADPRP residues 56-200 – Deinococcus radiodurans
3o8s - ADPRP – Streptococcus suis

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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Michal Harel, Alexander Berchansky

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