Fig. 2: Effect of different phosphorylating agents on βPGM.
From: Allomorphy as a mechanism of post-translational control of enzyme activity
a, b Overlays of a section of 1H15N-TROSY spectra highlighting the behaviour of residue A113. a βPGMWT (black) populates conformer A and conformer B in slow exchange. βPGMWT supplemented with F16BP (pink) populates phosphorylated conformer A (AP) as the dominant species, phosphorylated conformer B (BP) and a βPGMWT:F16BP species (A:F16BP). βPGMWT supplemented with βG16BP (green) populates an A:βG16BP complex. b βPGMP146A (black) populates one conformer (conformer B). βPGMP146A supplemented with F16BP (pink) populates conformer B and BP. βPGMP146A supplemented with βG16BP (green) populates a AP:G6P complex and a B:βG16BP complex. Peaks indicated by grey asterisks correspond to the βPGMWT:BeF3 complex (grey; δN = 133.5 ppm; BMRB 1785135), which is an analogue of AP, and the Mg2+-saturated βPGMD10N:βG16BP complex (grey; δN = 133.8 ppm; BMRB 2717431), which is a mimic of the A:βG16BP complex, and are shown for comparison.
