ArticleThe Biochemical journal2007
Crystal structure of human phosphoribosylpyrophosphate synthetase 1 reveals a novel allosteric site.
Article in The Biochemical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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57 citing papers in PubMed, 122 citations in OpenAlex.
- Biosynthesis of cyanophycin by high-cell-density cultivation of recombinant Escherichia coli for corrosion-resistant biomaterial applications.Bioprocess and biosystems engineering · 2026Article
- The molecular basis of ADP-ribose pyrophosphorylation by a phage PRPS-like enzyme in NAD+ reconstitution.Nucleic acids research · 2026Article
- Divergent evolution of the PRPS enzymes across the tree of life.bioRxiv : the preprint server for biology · 2026Article
- A preliminary study on the regulatory role of phosphoribosyl pyrophosphate synthetase 2 in vesicular stomatitis virus infection.Virus genes · 2026Article
- The role of gene duplication and paralog specialisation in the evolution of the mammalian PRPS complex.Nature communications · 2025Article
- PRPS activity tunes redox homeostasis in Myc-driven lymphoma.Redox biology · 2025Article
- PRPS2 enhances RNA mNature communications · 2025Article
- Direct stimulation of de novo nucleotide synthesis by O-GlcNAcylation.Nature chemical biology · 2024Article
- Review
- Dual role of lipids for genome stability and pluripotency facilitates full potency of mouse embryonic stem cells.Protein & cell · 2023Article
- Structural basis of human PRPS2 filaments.Cell & bioscience · 2023Article
- Human PRPS1 filaments stabilize allosteric sites to regulate activity.Nature structural & molecular biology · 2023Article
- PRPS2 mutations drive acute lymphoblastic leukemia relapse through influencing PRPS1/2 hexamer stability.Blood science (Baltimore, Md.) · 2023Article
- Identification of purine biosynthesis as an NADH-sensing pathway to mediate energy stress.Nature communications · 2022Article
- Article
- Review
- Biological synthesis of nicotinamide mononucleotide.Biotechnology letters · 2021Review
- Metabolic Changes Are Associated with Melphalan Resistance in Multiple Myeloma.Journal of proteome research · 2021Article
- Co-therapy with S-adenosylmethionine and nicotinamide riboside improves t-cell survival and function in Arts Syndrome (PRPS1 deficiency).Molecular genetics and metabolism reports · 2021Article
- NOTCH1-driven UBR7 stimulates nucleotide biosynthesis to promote T cell acute lymphoblastic leukemia.Science advances · 2021Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PRPP (phosphoribosylpyrophosphate) is an important metabolite essential for nucleotide synthesis and PRS (PRPP synthetase) catalyses synthesis of PRPP from R5P (ribose 5-phosphate) and ATP. The enzymatic activity of PRS is regulated by phosphate ions, divalent metal cations and ADP. In the present study we report the crystal structures of recombinant human PRS1 in complexes with SO4(2-) ions alone and with ATP, Cd2+ and SO4(2-) ions respectively. The AMP moiety of ATP binds at the ATP-binding site, and a Cd2+ ion binds at the active site and in a position to interact with the beta- and gamma-phosphates of ATP. A SO4(2-) ion, an analogue of the activator phosphate, was found to bind at both the R5P-binding site and the allosteric site defined previously. In addi-tion, an extra SO4(2-) binds at a site at the dimer interface between the ATP-binding site and the allosteric site. Binding of this SO4(2-) stabilizes the conformation of the flexible loop at the active site, leading to the formation of the active, open conformation which is essential for binding of ATP and initiation of the catalytic reaction. This is the first time that structural stabilization at the active site caused by binding of an activator has been observed. Structural and biochemical data show that mutations of some residues at this site influence the binding of SO4(2-) and affect the enzymatic activity. The results in the present paper suggest that this new SO4(2-)-binding site is a second allosteric site to regulate the enzymatic activity which might also exist in other eukaryotic PRSs (except plant PRSs of class II), but not in bacterial PRSs.
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