Journal
STRUCTURE
Volume 26, Issue 2, Pages 295-+Publisher
CELL PRESS
DOI: 10.1016/j.str.2018.01.004
Keywords
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Funding
- Biostruct-X
- Swedish Research Council
- Knut and Alice Wallenberg Foundation
- Wenner-Gren Foundation
- Goran Gustafsson Foundation
- Swedish Children's Cancer Foundation
- Swedish Pain Relief Foundation
- Torsten and Ragnar Soderberg Foundation
- Swedish Cancer Society
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Human NUDT22 belongs to the diverse NUDIX family of proteins, but has, until now, remained uncharacterized. Here we show that human NUDT22 is a Mg2+-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.
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