Structural highlights
Publication Abstract from PubMed
Human NUDT22 belongs to the diverse NUDIX family of proteins, but has, until now, remained uncharacterized. Here we show that human NUDT22 is a Mg(2+)-dependent UDP-glucose and UDP-galactose hydrolase, producing UMP and glucose 1-phosphate or galactose 1-phosphate. We present the structure of human NUDT22 alone and in a complex with the substrate UDP-glucose. These structures reveal a partially conserved NUDIX fold domain preceded by a unique N-terminal domain responsible for UDP moiety binding and recognition. The NUDIX domain of NUDT22 contains a modified NUDIX box identified using structural analysis and confirmed through functional analysis of mutants. Human NUDT22's distinct structure and function as a UDP-carbohydrate hydrolase establish a unique NUDIX protein subfamily.
Human NUDT22 Is a UDP-Glucose/Galactose Hydrolase Exhibiting a Unique Structural Fold.,Carter M, Jemth AS, Carreras-Puigvert J, Herr P, Martinez Carranza M, Vallin KSA, Throup A, Helleday T, Stenmark P Structure. 2018 Feb 6;26(2):295-303.e6. doi: 10.1016/j.str.2018.01.004. PMID:29413322[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Carter M, Jemth AS, Carreras-Puigvert J, Herr P, Martinez Carranza M, Vallin KSA, Throup A, Helleday T, Stenmark P. Human NUDT22 Is a UDP-Glucose/Galactose Hydrolase Exhibiting a Unique Structural Fold. Structure. 2018 Feb 6;26(2):295-303.e6. doi: 10.1016/j.str.2018.01.004. PMID:29413322 doi:http://dx.doi.org/10.1016/j.str.2018.01.004
