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Conformational changes required for H+/Cl− exchange mediated by a CLC transporter
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Conformational changes required for H+/Cl− exchange mediated by a CLC transporter
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Journal Article
Conformational changes required for H+/Cl− exchange mediated by a CLC transporter
2014
Overview
CLC-type H
+
/Cl
−
exchangers are known to be regulated by voltage and H
+
and Cl
−
concentrations, but their gating mechanism remains poorly understood. New data now suggest that transport by the CLCs is regulated by two gates that are functionally linked through structural rearrangements outside of the ion-transport pathway.
CLC-type exchangers mediate transmembrane Cl
−
transport. Mutations altering their gating properties cause numerous genetic disorders. However, their transport mechanism remains poorly understood. In conventional models, two gates alternatively expose substrates to the intra- or extracellular solutions. A glutamate was identified as the only gate in the CLCs, suggesting that CLCs function by a nonconventional mechanism. Here we show that transport in CLC-ec1, a prokaryotic homolog, is inhibited by cross-links constraining movement of helix O far from the transport pathway. Cross-linked CLC-ec1 adopts a wild-type–like structure, indicating stabilization of a native conformation. Movements of helix O are transduced to the ion pathway via a direct contact between its C terminus and a tyrosine that is a constitutive element of the second gate of CLC transporters. Therefore, the CLC exchangers have two gates that are coupled through conformational rearrangements outside the ion pathway.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Biological Transport - physiology
/ Chloride Channels - chemistry
/ Chloride Channels - genetics
/ Chloride Channels - physiology
/ Escherichia coli K12 - metabolism
/ Escherichia coli Proteins - chemistry
/ Escherichia coli Proteins - genetics
/ Escherichia coli Proteins - physiology
/ Gates
/ Mutation
/ Proteins
