InterPro domain: IPR036157

This entry represents a distorted barrel domain found in deoxyuridine triphosphate nucleotidohydrolases and CTP deaminases.

Deoxyuridine triphosphate nucleotidohydrolase (dUTPase) cleaves dUTP into pyrophosphate and dUMP. Three different subunit organisations of dUTPases have been found: they are either monomers, dimers or trimers [ 1 ]. dUTPases from E. coli [ 2 ], human [ 3 ], and some virus [ 4 ] all share a common distorted barrel fold and form trimers [ 5 ]. In the homotrimer, each subunit folds into a twisted antiparallel beta-barrel with the N and C-terminal portions interacting with adjacent subunits [ 6 ].

CTP deaminase is a member of the family of the structurally related trimeric dUTPases and the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii [ 6 ].

The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases. It consists of three domain, domains I and II having a dUTPase fold [ 7 ].

1. Atomic resolution structure of Escherichia coli dUTPase determined ab initio. Acta Crystallogr. D Biol. Crystallogr. 57, 767-74
2. Crystal structure of the Escherichia coli dUTPase in complex with a substrate analogue (dUDP). Nat. Struct. Biol. 3, 532-8
3. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Structure 4, 1077-92
4. Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex. J. Mol. Biol. 285, 655-73
5. Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism. J. Mol. Biol. 341, 503-17
6. Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. J. Biol. Chem. 280, 3051-9
7. The monomeric dUTPase from Epstein-Barr virus mimics trimeric dUTPases. Structure 13, 1299-310