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Human NUDT22 Is a UDP-Glucose/Galactose Hydrolase Exhibiting a Unique Structural Fold
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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Number of Authors: 9
2018 (English)In: Structure, ISSN 0969-2126, E-ISSN 1878-4186, Vol. 26, no 2, p. 295-303Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2018. Vol. 26, no 2, p. 295-303
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Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-153774DOI: 10.1016/j.str.2018.01.004ISI: 000424806800012PubMedID: 29413322OAI: oai:DiVA.org:su-153774DiVA, id: diva2:1192356
Available from: 2018-03-22 Created: 2018-03-22 Last updated: 2018-03-22Bibliographically approved

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Martínez Carranza, MarkelStenmark, Pål
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