ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2021
New structural insights reveal an expanded reaction cycle for inositol pyrophosphate hydrolysis by human DIPP1.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 28 citations in OpenAlex.
- Three phosphatase families form a community: The phosphohydrolases that act upon inositol pyrophosphates.FEBS letters · 2026Review
- The Diphosphoinositol Polyphosphate Phosphohydrolase 1 family binds IPInternational journal of biological macromolecules · 2026Article
- Article
- Optimization of a high throughput screening platform to identify inhibitors of asymmetric diadenosine polyphosphatases.Analytical biochemistry · 2025Article
- Visualizing and Identifying Inositol Pyrophosphate Isomers in Crystallo.Methods in molecular biology (Clifton, N.J.) · 2025Article
- A fusion protein of polyphosphate kinase 1 (PPK1) and a Nudix hydrolase is involved in inorganic polyphosphate accumulation in the unicellular red alga Cyanidioschyzon merolae.Plant molecular biology · 2024Article
- Inositol pyrophosphate catabolism by three families of phosphatases regulates plant growth and development.PLoS genetics · 2024Article
- Article
- Biochemical and structural characterization of an inositol pyrophosphate kinase from a giant virus.The EMBO journal · 2024Article
- Fluorination Influences the Bioisostery of Myo-Inositol Pyrophosphate Analogs.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Inositol pyrophosphate dynamics reveals control of the yeast phosphate starvation program through 1,5-IPeLife · 2023Article
- Duf89 abets lncRNA control of fission yeast phosphate homeostasis via its antagonism of precocious lncRNA transcription termination.RNA (New York, N.Y.) · 2023Article
- Inositol Pyrophosphate-Controlled Kinetochore Architecture and Mitotic Entry inJournal of fungi (Basel, Switzerland) · 2022Article
- Structural and catalytic analyses of the InsPFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Development of Novel IP6K Inhibitors for the Treatment of Obesity and Obesity-Induced Metabolic Dysfunctions.Journal of medicinal chemistry · 2022Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Nudix hydrolases attract considerable attention for their wide range of specialized activities in all domains of life. One particular group of Nudix phosphohydrolases (DIPPs), through their metabolism of diphosphoinositol polyphosphates (PP-InsPs), regulates the actions of these polyphosphates upon bioenergetic homeostasis. In the current study, we describe, at an atomic level, hitherto unknown properties of human DIPP1.We provide X-ray analysis of the catalytic core of DIPP1 in crystals complexed with either natural PP-InsPs, alternative PP-InsP stereoisomers, or non-hydrolysable methylene bisphosphonate analogs ("PCP-InsPs"). The conclusions that we draw from these data are interrogated by studying the impact upon catalytic activity upon mutagenesis of certain key residues. We present a picture of a V-shaped catalytic furrow with overhanging ridges constructed from flexible positively charged side chains; within this cavity, the labile phosphoanhydride bond is appropriately positioned at the catalytic site by an extensive series of interlocking polar contacts which we analogize as "suspension cables." We demonstrate functionality for a triglycine peptide within a β-strand which represents a non-canonical addition to the standard Nudix catalytic core structure. We describe pre-reaction enzyme/substrate states which we posit to reflect a role for electrostatic steering in substrate capture. Finally, through time-resolved analysis, we uncover a chronological sequence of DIPP1/product post-reaction states, one of which may rationalize a role for InsP
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