Figure 4
From: Energetics and Structural Characterization of the large-scale Functional Motion of Adenylate Kinase
Characterization of the AK functional mechanism.
(a) The molecular structures corresponding to the main free-energy minima A (open conformation) and B (closed conformation) states. The conformations are superimposed on the open and closed X-ray structures11,21. The LID and NMP domains are colored in green and yellow, respectively for the free-energy minima states and in pink for the X-ray structures. (b) The FES of the AK closed/open transition is shown as a function of LID domain closed to open transition (x axis) and NMP domain closed to open transition (y axis). Isosurfaces are shown each 2.5 kJ/mol. Different conformations of LID and NMP domains are represented in insets 1 to 3. The LID and NMP domains are depicted in green and yellow, respectively. (c) The lowest free-energy path of AK opening is represented in insets I to III. The LID and NMP domains are depicted in green and yellow, respectively.
