Fig. 5: Structure of Synechocystis F/SBPase showing peptide coverage and affected peptides from LiP-SMap.
From: Metabolite interactions in the bacterial Calvin cycle and implications for flux regulation
a Structure of F/SBPase as a homotetramer from Protein Databank reference 3RPL55. The substrate fructose-1,6-bisphosphate is shown in blue sticks and active site Mg2+ ions as red spheres. The allosteric inhibitor AMP binds at the central interface of the tetramer and is shown as yellow sticks. b Monomer of F/SBPase colored according to different structural elements, showing interaction with fructose-1,6-bisphosphate and AMP molecules. c Uppler left panel shows a monomer of F/SBPase with peptides detected by LC-MS as colored ribbons. Peptides that were not detected are gray ribbons. Right panels outline which peptides were affected by the indicated metabolite.
