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Structure paper

TitleStructure of the CLC-1 chloride channel from .
Journal, issue, pagesElife, Vol. 7, Year 2018
Publish dateMay 29, 2018
AuthorsEunyong Park / Roderick MacKinnon /
PubMed AbstractCLC channels mediate passive Cl conduction, while CLC transporters mediate active Cl transport coupled to H transport in the opposite direction. The distinction between CLC-0/1/2 channels and CLC ...CLC channels mediate passive Cl conduction, while CLC transporters mediate active Cl transport coupled to H transport in the opposite direction. The distinction between CLC-0/1/2 channels and CLC transporters seems undetectable by amino acid sequence. To understand why they are different functionally we determined the structure of the human CLC-1 channel. Its 'glutamate gate' residue, known to mediate proton transfer in CLC transporters, adopts a location in the structure that appears to preclude it from its transport function. Furthermore, smaller side chains produce a wider pore near the intracellular surface, potentially reducing a kinetic barrier for Cl conduction. When the corresponding residues are mutated in a transporter, it is converted to a channel. Finally, Cl at key sites in the pore appear to interact with reduced affinity compared to transporters. Thus, subtle differences in glutamate gate conformation, internal pore diameter and Cl affinity distinguish CLC channels and transporters.
External linksElife / PubMed:29809153 / PubMed Central
MethodsEM (single particle)
Resolution3.36 Å
Structure data

7544

6coy

EMDB-7544, PDB-6coy:
Human CLC-1 chloride ion channel, transmembrane domain
Method: EM (single particle) / Resolution: 3.36 Å

7545

6coz

EMDB-7545, PDB-6coz:
Human CLC-1 chloride ion channel, C-terminal cytosolic domain
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

ChemComp-CL:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / chloride / channel / CLC

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