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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Phosphoribosyl pyrophosphate synthetase (PRPS) is a conserved enzyme crucial for nucleotide metabolism.
  • Mutations in human PRPS1 are linked to various diseases.
  • PRPS enzymes assemble into filaments across different species.

Purpose of the Study:

  • To determine the structures of human PRPS1 filaments in active and inhibited states.
  • To investigate the role of filament assembly in PRPS1 activity and regulation.
  • To understand the structural basis of PRPS1-associated diseases.

Main Methods:

  • X-ray crystallography to determine high-resolution structures of PRPS1 filaments.
  • Biochemical assays to assess enzyme activity and substrate turnover.
  • Analysis of disease-associated mutations in relation to filament structure.

Main Results:

  • Human PRPS1 forms filaments with fixed assembly contacts that accommodate different conformational states.
  • Filament assembly stabilizes the activator phosphate binding site, enhancing enzyme activity.
  • Disease-linked mutations were found to disrupt filament assembly, correlating with altered activity.
  • Structures revealed coupled catalysis and product release between adjacent active sites within the filament.

Conclusions:

  • PRPS1 filamentation provides a conserved, evolutionarily ancient mechanism for allosteric regulation of nucleotide metabolism.
  • Filament stability is critical for PRPS1 activity, and its disruption contributes to disease pathogenesis.
  • Assembly-based regulation of enzyme activity represents a diverse strategy for maintaining metabolic homeostasis.