ADP-ribose pyrophosphatase
From Proteopedia
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<StructureSection load='1khz' size='450' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'> | <StructureSection load='1khz' size='450' side='right' scene='48/488514/Cv/1' caption='ADP-ribose pyrophosphatase dimer complex with methylene ADP-ribose, Cl- (large green) and Mg+2 (small green) ions, [[1khz]]'> | ||
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== Function == | == 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.<ref>PMID:11323725</ref> ADPRP belongs to the family of NUDIX hydrolase. | + | '''ADP-ribose pyrophosphatase''' (ADPRP) or '''ADPRase''' 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.<ref>PMID:11323725</ref> ADPRP belongs to the family of NUDIX hydrolase. |
== Structural highlights == | == Structural highlights == | ||
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</StructureSection> | </StructureSection> | ||
| - | ==3D structures of ADP-ribose pyrophosphatase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *ADP-ribose pyrophosphatase | ||
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| - | **[[1q33]] – hADPRP NUDT9 residues 59-350 – human<br /> | ||
| - | **[[1v8i]], [[3x0i]], [[3x0j]], [[3x0l]], [[3x0n]], [[3x0p]], [[3x0q]], [[3x0s]] - TtADPRP – ''Thermus thermophilus''<br /> | ||
| - | **[[3x0k]], [[3k0l]] - TtADPRP ES-state <br /> | ||
| - | **[[3x0m]], [[3k0n]] - TtADPRP ESM-state <br /> | ||
| - | **[[3x0o]], [[3k0p]], [[3k0q]] - TtADPRP ESMM-state <br /> | ||
| - | **[[3x0r]], [[3k0s]] - TtADPRP E'-state <br /> | ||
| - | **[[2w4e]] – ADPRP residues 56-200 – ''Deinococcus radiodurans''<br /> | ||
| - | **[[3o8s]] - ADPRP – ''Streptococcus suis''<br /> | ||
| - | **[[4kyx]] – ADPRP Mutt – ''Rickettsia felis''<br /> | ||
| - | **[[5i8u]] - ADPRP – ''Mycobacterium tuberculosis''<br /> | ||
| - | **[[1viq]], [[1viu]] - EcADPRP – ''Escherichia coli''<br /> | ||
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| - | *ADP-ribose pyrophosphatase binary complex | ||
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| - | **[[1v8l]] – TtADPRP + ADPR<br /> | ||
| - | **[[1v8n]] - TtADPRP + Zn<br /> | ||
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| - | *ADP-ribose pyrophosphatase ternary complex | ||
| - | **[[1khz]] - EcADPRP + AMPCPR + Mg <br /> | ||
| - | **[[1qvj]] - hADPRP + ribose-5-phosphate + Mg<br /> | ||
| - | **[[1v8m]] - TtADPRP + Gd + ADPR <br /> | ||
| - | **[[1v8s]] - TtADPRP + AMP + Mg<br /> | ||
| - | **[[1v8t]] - TtADPRP + ribose-5-phosphate + Zn<br /> | ||
| - | **[[1v8u]] - TtADPRP (mutant) + sulfate + Mg<br /> | ||
| - | **[[1v8v]] - TtADPRP (mutant) + ADPR + Mg<br /> | ||
| - | **[[1v8w]] - TtADPRP (mutant) + sulfate + Zn<br /> | ||
| - | **[[1v8y]] - TtADPRP (mutant) + ADPR + Zn<br /> | ||
| - | **[[1v8r]] - TtADPRP + ADPR + Zn<br /> | ||
| - | **[[3bm4]] - hADPRP NUDT5 + AMPCPR + Mg<br /> | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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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
- ↑ 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
