ArticleProceedings of the National Academy of Sciences of the United States of America2016
An HD domain phosphohydrolase active site tailored for oxetanocin-A biosynthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 32 citations in OpenAlex.
- The cobalamin-binding domain of cobalamin-dependent radical S-adenosylmethionine enzymes: Familiarity in unfamiliar places.Journal of inorganic biochemistry · 2026Review
- A [2.1.0]-Fused Bicyclic Intermediate Is Produced during the Biosynthesis of Oxetane Nucleosides.Journal of the American Chemical Society · 2025Article
- Reaction Mechanism and Metal Selectivity of Human SAMHD1 Elucidated by QM/MM Calculations.ACS catalysis · 2025Article
- Changing Fates of the Substrate Radicals Generated in the Active Sites of the BJournal of the American Chemical Society · 2023Article
- Article
- Cobalamin-Dependent RadicalACS bio & med chem Au · 2022Review
- Studies of GenK and OxsB, two BMethods in enzymology · 2022Article
- How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA.Nature communications · 2021Article
- Biosynthesis of Oxetanocin-A Includes a BBiochemistry · 2021Article
- The HD-Domain Metalloprotein Superfamily: An Apparent Common Protein Scaffold with Diverse Chemistries.Catalysts (Basel, Switzerland) · 2020Article
- HD-[HD-GYP] Phosphodiesterases: Activities and Evolutionary Diversification within the HD-GYP Family.Biochemistry · 2020Article
- Inorganic Pyrophosphatase-Nanodiamond Conjugates Hydrolyze Pyrophosphate in Human Synovial Fluid.ACS omega · 2020Article
- Identification and Heterologous Expression of the Albucidin Gene Cluster from the Marine StrainMicroorganisms · 2020Article
- DNA processing by the MOBH family relaxase TraI encoded within the gonococcal genetic island.Nucleic acids research · 2019Article
- Bioinformatic Exploration of Metal-Binding Proteome of Zoonotic PathogenFrontiers in genetics · 2019Article
- C-C bond forming radical SAM enzymes involved in the construction of carbon skeletons of cofactors and natural products.Natural product reports · 2018Review
- A BNature · 2017Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
HD domain phosphohydrolase enzymes are characterized by a conserved set of histidine and aspartate residues that coordinate an active site metallocenter. Despite the important roles these enzymes play in nucleotide metabolism and signal transduction, few have been both biochemically and structurally characterized. Here, we present X-ray crystal structures and biochemical characterization of the Bacillus megaterium HD domain phosphohydrolase OxsA, involved in the biosynthesis of the antitumor, antiviral, and antibacterial compound oxetanocin-A. These studies reveal a previously uncharacterized reaction for this family; OxsA catalyzes the conversion of a triphosphorylated compound into a nucleoside, releasing one molecule of inorganic phosphate at a time. Remarkably, this functionality is a result of the OxsA active site, which based on structural and kinetic analyses has been tailored to bind the small, four-membered ring of oxetanocin-A over larger substrates. Furthermore, our OxsA structures show an active site that switches from a dinuclear to a mononuclear metal center as phosphates are eliminated from substrate.
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