5LOU

human NUDT22

Summary for 5LOU

• Entry DOI: 10.2210/pdb5lou/pdb
• Descriptor: Nucleoside diphosphate-linked moiety X motif 22, PHOSPHATE ION (3 entities in total)
• Functional Keywords: nudix, hydrolase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 71240.04

Authors

Carter, M.,Stenmark, P. (deposition date: 2016-08-10, release date: 2017-09-13, Last modification date: 2024-05-08)

Primary citation

Carter, M.,Jemth, A.S.,Carreras-Puigvert, J.,Herr, P.,Martinez Carranza, M.,Vallin, K.S.A.,Throup, A.,Helleday, T.,Stenmark, P.
Human NUDT22 Is a UDP-Glucose/Galactose Hydrolase Exhibiting a Unique Structural Fold.
Structure, 26:295-303.e6, 2018

PubMed Abstract: 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-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.

PubMed: 29413322
DOI: 10.1016/j.str.2018.01.004

Experimental method

X-RAY DIFFRACTION (1.8 Å)