Fig 7. Hypothesized impacts of ScHxk2^G238V on the catalytic mechanism.

(A) The G238V mutation alters the dynamics of the β9/β10 β-hairpin, the catalytic D211 residue, and the ɑ11’ helix. The implications of these changes on enzyme function are summarized. (B) Two conformations taken from the ScHxk2^G238V apo simulations highlight the movements of V236 (loop residue) and D211 (catalytic residue). In blue, V236 is shown in an open-like conformation, and D211 is shown in a glucose-ready conformation. In pink, V236 is shown in a closed-like conformation, and D211 is shown in a displaced conformation. Key secondary-structure elements are labeled with text, and the substrate-adjacent loop is labeled by its residues (I231-V236). The QR code provides a link to an online ProteinVR scene for virtual-reality visualization. (C) The distributions of the V236 χ₁ dihedral angle. For reference, the red and green dashed lines show the corresponding values of the 1IG8 (ScHxk2, open) and 3O8M (KlHxk1, closed) crystal structures, respectively.