Figure 2.

(Left side) Schematic representation of open (O, states 1 and 2) and closed (C, states 3–5) state structures describing GK's enzymatic reaction pathway. (Right side) Average RMS fluctuation measurements from 20-ns MD trajectories reported for each state (shading highlights flexible and rigid parts). GMP/GDP and ATP/ADP nucleotides as well as magnesium are shown both schematically and as van der Waals spheres. State 6 describes a putative stable form of the closed apo (C_APO) GK and is considered off the proposed enzymatic pathway.