Figure 1: Kinetic and structural models for substrate binding by AK.
From: Overlap between folding and functional energy landscapes for adenylate kinase conformational change
(a) Nucleotide binding mechanism for AK. E corresponds to enzyme, S to substrate, ESO to a transient substrate-bound encounter complex, ESC to the active conformation of AK. Superscripts 'O' and 'C' refer to AK in open (inactive) and closed (active) conformations. The rate constants for association and dissociation of ESO are given by kon and koff, whereas the rate constants for conformational change are given by kclose and kopen. (b, c) Structures of AKe during the extreme stages of catalysis. ATPlid (residues 113–176) and AMPlid (residues 28–72) are coloured gold and the INSERT segment of the ATPlid (residues 122–15943) is coloured blue. (b) Substrate-free open AKe (4AKE.pdb). Residues isoleucine 116 and leucine168, which are mutated into glycine in this study, are highlighted with ball and stick representations, and the location of alpha helices, α6 and α7, is indicated. (c) Closed AKe with bound Ap5A (1AKE.pdb). All molecular graphic images in this report were prepared with MolMol44.
