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Structure paper

TitleStructure of the human ClC-1 chloride channel.
Journal, issue, pagesPLoS Biol, Vol. 17, Issue 4, Page e3000218, Year 2019
Publish dateApr 25, 2019
AuthorsKaituo Wang / Sarah Spruce Preisler / Liying Zhang / Yanxiang Cui / Julie Winkel Missel / Christina Grønberg / Kamil Gotfryd / Erik Lindahl / Magnus Andersson / Kirstine Calloe / Pascal F Egea / Dan Arne Klaerke / Michael Pusch / Per Amstrup Pedersen / Z Hong Zhou / Pontus Gourdon /
PubMed AbstractClC-1 protein channels facilitate rapid passage of chloride ions across cellular membranes, thereby orchestrating skeletal muscle excitability. Malfunction of ClC-1 is associated with myotonia ...ClC-1 protein channels facilitate rapid passage of chloride ions across cellular membranes, thereby orchestrating skeletal muscle excitability. Malfunction of ClC-1 is associated with myotonia congenita, a disease impairing muscle relaxation. Here, we present the cryo-electron microscopy (cryo-EM) structure of human ClC-1, uncovering an architecture reminiscent of that of bovine ClC-K and CLC transporters. The chloride conducting pathway exhibits distinct features, including a central glutamate residue ("fast gate") known to confer voltage-dependence (a mechanistic feature not present in ClC-K), linked to a somewhat rearranged central tyrosine and a narrower aperture of the pore toward the extracellular vestibule. These characteristics agree with the lower chloride flux of ClC-1 compared with ClC-K and enable us to propose a model for chloride passage in voltage-dependent CLC channels. Comparison of structures derived from protein studied in different experimental conditions supports the notion that pH and adenine nucleotides regulate ClC-1 through interactions between the so-called cystathionine-β-synthase (CBS) domains and the intracellular vestibule ("slow gating"). The structure also provides a framework for analysis of mutations causing myotonia congenita and reveals a striking correlation between mutated residues and the phenotypic effect on voltage gating, opening avenues for rational design of therapies against ClC-1-related diseases.
External linksPLoS Biol / PubMed:31022181 / PubMed Central
MethodsEM (single particle)
Resolution3.63 - 4.34 Å
Structure data

4645

6qv6

EMDB-4645, PDB-6qv6:
CryoEM structure of the human ClC-1 chloride channel, membrane domain
Method: EM (single particle) / Resolution: 3.63 Å

4646

6qvb

EMDB-4646, PDB-6qvb:
CryoEM structure of the human ClC-1 chloride channel, CBS state 3
Method: EM (single particle) / Resolution: 4.34 Å

4647

6qvc

EMDB-4647, PDB-6qvc:
CryoEM structure of the human ClC-1 chloride channel, CBS state 1
Method: EM (single particle) / Resolution: 4.0 Å

4649

6qvd

EMDB-4649, PDB-6qvd:
CryoEM structure of the human ClC-1 chloride channel, CBS state 2
Method: EM (single particle) / Resolution: 4.34 Å

4657

6qvu

EMDB-4657, PDB-6qvu:
CryoEM structure of the human ClC-1 chloride channel, low pH
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / chloride channel / CLC1 / CLCN1

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