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TitleMolecular insights into the human CLC-7/Ostm1 transporter.
Journal, issue, pagesSci Adv, Vol. 6, Issue 33, Page eabb4747, Year 2020
Publish dateAug 12, 2020
AuthorsSensen Zhang / Yang Liu / Bing Zhang / Jun Zhou / Tianyu Li / Zhiqiang Liu / Yang Li / Maojun Yang /
PubMed AbstractCLC family proteins translocate chloride ions across cell membranes to maintain the membrane potential, regulate the transepithelial Cl transport, and control the intravesicular pH among different ...CLC family proteins translocate chloride ions across cell membranes to maintain the membrane potential, regulate the transepithelial Cl transport, and control the intravesicular pH among different organelles. CLC-7/Ostm1 is an electrogenic Cl/H antiporter that mainly resides in lysosomes and osteoclast ruffled membranes. Mutations in human CLC-7/Ostm1 lead to lysosomal storage disorders and severe osteopetrosis. Here, we present the cryo-electron microscopy (cryo-EM) structure of the human CLC-7/Ostm1 complex and reveal that the highly glycosylated Ostm1 functions like a lid positioned above CLC-7 and interacts extensively with CLC-7 within the membrane. Our complex structure reveals a functionally crucial domain interface between the amino terminus, TMD, and CBS domains of CLC-7. Structural analyses and electrophysiology studies suggest that the domain interaction interfaces affect the slow gating kinetics of CLC-7/Ostm1. Thus, our study deepens understanding of CLC-7/Ostm1 transporter and provides insights into the molecular basis of the disease-related mutations.
External linksSci Adv / PubMed:32851177 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

30238

7bxu

EMDB-30238, PDB-7bxu:
CLC-7/Ostm1 membrane protein complex
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / complex / lysosome / transporter

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