Nudix family

NUDIX
Structure of MT-ADPRase, a Nudix hydrolase from Mycobacterium tuberculosis
Identifiers
Symbol	NUDIX
Pfam	PF00293
Pfam clan	CL0261
InterPro	IPR000086
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

NUDIX-like
Crystal structure of NADH pyrophosphatase (1790429) from Escherichia coli k12 at 2.20 a resolution
Identifiers
Symbol	NUDIX-like
Pfam	PF09296
Pfam clan	CL0261
InterPro	IPR015375
SCOP	1vk6
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

The Nudix family is a protein family of phosphohydrolases.^[1][2][3] Using water-mediated catalysis they break a phosphate bond in their substrate to create two products. Nudix stands for Nucleoside Diphosphate linked to X. There are two components to the Nudix family: the so-called Nudix fold of a beta sheet with alpha helices on each side and the Nudix motif which contains catalytic and metal-binding amino acids. The Nudix motif is GXXXXXEXXXXXXXREUXEEXGU where U is Isoleucine, Leucine, or Valine and X is any amino acid. This forms a short helix which (usually) contains the catalytic amino acids. Nudix family enzymes include Dcp2 of the decapping complex, ADP-ribose diphosphatase, MutT, ADPRase, Ap4A, RppH, and many others.^[4]

References

1. ^ Bessman MJ, Frick DN, O'Handley SF (October 1996). "The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes". J. Biol. Chem. 271 (41): 25059–62. doi:10.1074/jbc.271.41.25059. PMID 8810257. 
2. ^ Mildvan AS, Xia Z, Azurmendi HF, et al. (January 2005). "Structures and mechanisms of Nudix hydrolases". Arch. Biochem. Biophys. 433 (1): 129–43. doi:10.1016/j.abb.2004.08.017. PMID 15581572. 
3. ^ McLennan AG (January 2006). "The Nudix hydrolase superfamily". Cell. Mol. Life Sci. 63 (2): 123–43. doi:10.1007/s00018-005-5386-7. PMID 16378245. 
4. ^ Mildvan, A.S.; Xia, Z.; Azurmendi, H.F.; Saraswat, V.; Legler, P.M.; Massiah, M.A.; Gabelli, S.B.; Bianchet, M.A. et al. (2005). "Structures and mechanisms of Nudix hydrolases". Archives of Biochemistry and Biophysics 433 (1): 129–143. doi:10.1016/j.abb.2004.08.017. PMID 15581572. http://linkinghub.elsevier.com/retrieve/pii/S0003986104004667