
PRPS1 assembles for allosteric activation
A series of cryo-EM structures of PRPS1 reveal formation of D3 symmetric hexamers, which assemble into filaments, stabilising allosteric sites within the enzyme and promoting its activation.
A series of cryo-EM structures of PRPS1 reveal formation of D3 symmetric hexamers, which assemble into filaments, stabilising allosteric sites within the enzyme and promoting its activation.