Fig. 3: Structural basis for ATP recognition.
From: Comprehensive profiling of the catalytic conformations of human Guanylate kinase
a Histogram of ATPγS-induced chemical shift perturbations in GMPK at a molar ratio of 2:1. b Mapping of ATPγS-induced CSPs larger than mean plus 2σ (red) onto the apo state of the GMPK. c Cartoon representation of the GMPK-GMP-ATPγS complex structure with the mFo-DFc omit map density (black mesh) for GMP and ATPγS contoured at 3σ. d Electrostatic surface potential of the GMPK-GMP-ATPγS complex. e Structural superposition of GMPK-GMP-ATPγS and GMPK-ADP. pink: GMPK-ADP, aquamarine: GMPK-GMP-ATPγS. f Detailed view of the adenine moiety and α/β -phosphate moiety interactions with GMPK with dashed lines indicating interatomic distances. g Detailed view of the γ-phosphate moiety interactions with GMPK. h Binding affinity between GMPK mutants with ATPγS as determined by ITC with fitted values and errors presented. i Kinetic parameters (KM, kcat and kcat/KM) for ATP were determined for both the wild-type and mutant GMPK. N.D. indicates no detectable activity.
