Abstract
The proton-activated chloride (PAC) channel plays a key role in determining the acid toxicity to mammalian cells. However, the mechanism underlies its pH-sensing function remains unclear. We analyzed the PAC channel in nanodisc using single-particle cryo-electron microscopy (cryo-EM) and revealed structures of PAC at two different pH conditions (pH8 and pH4). The homo-trimeric PAC channel contains a transmembrane domain (TMD) with two helices and an extracellular domain (ECD). Environmental acidification induces a major conformational rearrangement in the TMD and TMD-ECD interface, including a compression dynamics of the channel complex and a domain-swapping movement of the TM1.
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