Fig. 1: Cryo-EM and mechanistic studies of LdGDP-MP.
From: Structural insights into selective inhibition of leishmanial GDP-mannose pyrophosphorylase
a Overall views of hexameric LdGDP-MP with six subunits colored differently. The real density maps are shown in grey mesh. b Ribbon diagrams of a LdGDP-MP monomer. c Detailed interface contacts between neighboring subunits. d, e Magnified views of GTP- (d) or GDP-Man- (e) binding pocket with the real density map of GTP or GDP-Man shown in mesh. f Catalytic center of LdGDP-MP. g Activity comparisons of LdGDP-MP with mutants as labeled. h Impacts on the enzyme activity upon mutations for disrupting the interface-1 of LdGDP-MP. i Proposed evolutionary pathway of GDP-MPs from bacteria to human in terms of activity modulation. All enzyme assays were repeated at least three times and data were shown as means ± SD.
