Structural elements of cyanobacterial co-factor-independent phosphoglycerate mutase that mediate regulation by PirC.

ABSTRACT: The 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM) has been identified as a regulating key point in the carbon storage metabolism of cyanobacteria. Upon nitrogen starvation, the iPGAM is inhibited by the P_II-interacting regulator PirC, which is released from its interaction partner P_II due to elevated 2-oxoglutarate levels. In silico analysis of 338 different iPGAMs revealed a deep-rooted distinctive evolution of iPGAMs in cyanobacteria. Remarkably, cyanobacterial iPGAMs possess a unique loop structure and an extended C-terminus. Our mass photometry analysis suggests that iPGAM forms a complex with three individual PirC monomers. Biolayer interferometry revealed that the PirC-iPGAM complex is affected by the unique loop and the C-terminal s

SUBMITTER: Orthwein T 

PROVIDER: S-EPMC12077085 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature