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.
A cardinal rule of DNA replication is to prevent any possibility of pre-replication complexes re-loading during S phase, risking genotoxic over-replication. But can this rule be broken in emergency situations to preserve genome integrity?