2e5x

Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3Structure of nucleotide triphosphate pyrophosphatase from pyrococcus horikoshii OT3

Structural highlights

2e5x is a 1 chain structure with sequence from Pyrococcus horikoshii OT3. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

IXTPA_PYRHO Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.[HAMAP-Rule:MF_01405]^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Lokanath NK, Pampa KJ, Takio K, Kunishima N. Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3: functional significance of interprotomer conformational changes. J Mol Biol. 2008 Jan 25;375(4):1013-25. Epub 2007 Nov 13. PMID:18062990 doi:10.1016/j.jmb.2007.11.018

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OCA

[1] Lokanath NK, Pampa KJ, Takio K, Kunishima N. Structures of dimeric nonstandard nucleotide triphosphate pyrophosphatase from Pyrococcus horikoshii OT3: functional significance of interprotomer conformational changes. J Mol Biol. 2008 Jan 25;375(4):1013-25. Epub 2007 Nov 13. PMID:18062990 doi:10.1016/j.jmb.2007.11.018

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