Fig. 6: Conformational Dynamics of hAE3 During Substrate Transport.
From: The structural insight into the functional modulation of human anion exchanger 3
a The comparative analysis of the hAE3 outward- and inward-facing conformations. The cryo-EM structure of \({{\rm{hAE}}}{3}^{{{{\rm{HCO}}}}_{3}-}\) was aligned with the homology -based model depicting its inward-facing state. The remarkable movements of the helices were indicated with arrows. b The outer and inner vestibules were shown in the AE3 structures in the outward- and inward-facing conformations, respectively. The cryo-EM structure of \({{\rm{hAE}}}{3}^{{{{\rm{HCO}}}}_{3}-}\) and the homology-based model of AE3 in the inward-facing conformation were shown as the solvent-accessible electrostatic surface–potential maps, cut away to reveal the vestibules. The key substrate-binding residue, R1052, is depicted in a stick model, color-coded by atomic element, underscoring its role in substrate coordination.
