Abstract
The zinc/proton antiporter YiiP from Escherichia coli, a member of the cation diffusion facilitator family, plays an important role in maintaining cellular Zn2+ homeostasis. The difference between experimental inward-facing (IF) and outward-facing (OF) structures suggested a transport model involving large-scale scissoring of the transmembrane domains (TMDs). However, several experiments on YiiP and its mammalian homolog ZnT8 showed that this scissor-like rotation was not necessary for transport activity.
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