Fig. 5: Structural basis of reversible phosphoryl transfer reactions.
From: Comprehensive profiling of the catalytic conformations of human Guanylate kinase
a Structural superposition of the GMPK-GDP-ADP and GMPK-GMP-ATPγS complexes. b Interaction of the GDP β-phosphate with GMPK. c ITC analysis of GMPK mutants binding to GDP. d Reverse reaction recorded at different time points by 1H NMR. e Cartoon representation of the GMPK-GMP-ADP-AlF4--Mg2+-K+ complex with the mFo-DFc omit map density (black mesh) for GMP, ADP, AlF4-, Mg2+ and K+ contoured at 3σ. f AlF4- and magnesium ion binding site. Potassium ion is depicted as purple sphere, water molecule as red sphere, magnesium ion as green sphere and AlF4- is shown in stick representation. g Structural superposition of the transition state analogue and GMPK-GMP-ATPγS-K+ complexes. h Proposed catalysis model of GMPK.
