Fig. 5
From: Uncoupling conformational states from activity in an allosteric enzyme
Crystal structure and native IM-MS of apo-, l-His-bound and TIH-bound ATP-PRT. Cartoon representation of the allosteric binding site in the hexamer, surface representation viewed from the top and native drift time distribution of: a, b, c Apo- (PDB code 1NH7); d, e, f l-His-bound (PDB code 5LHU), and g, h, i TIH-bound (PDB code 5LHT) ATP-PRT. Allosteric domains are coloured in yellow while the catalytic domains are coloured in blue. The bars represent the span of the different molecule complexes. Distances have been measured between coupled Cα atoms of I269 (yellow bars) and I129 (blue bars). The black arrow on c indicates the fraction of unliganded ATP-PRT in the T-state
