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TitleAtomic structure of the innexin-6 gap junction channel determined by cryo-EM.
Journal, issue, pagesNat Commun, Vol. 7, Page 13681, Year 2016
Publish dateDec 1, 2016
AuthorsAtsunori Oshima / Kazutoshi Tani / Yoshinori Fujiyoshi /
PubMed AbstractInnexins, a large protein family comprising invertebrate gap junction channels, play an essential role in nervous system development and electrical synapse formation. Here we report the cryo-electron ...Innexins, a large protein family comprising invertebrate gap junction channels, play an essential role in nervous system development and electrical synapse formation. Here we report the cryo-electron microscopy structures of Caenorhabditis elegans innexin-6 (INX-6) gap junction channels at atomic resolution. We find that the arrangements of the transmembrane helices and extracellular loops of the INX-6 monomeric structure are highly similar to those of connexin-26 (Cx26), despite the lack of significant sequence similarity. The INX-6 gap junction channel comprises hexadecameric subunits but reveals the N-terminal pore funnel, consistent with Cx26. The helix-rich cytoplasmic loop and C-terminus are intercalated one-by-one through an octameric hemichannel, forming a dome-like entrance that interacts with N-terminal loops in the pore. These observations suggest that the INX-6 cytoplasmic domains are cooperatively associated with the N-terminal funnel conformation, and an essential linkage of the N-terminal with channel activity is presumably preserved across gap junction families.
External linksNat Commun / PubMed:27905396 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.6 Å
Structure data

EMDB-9570, PDB-5h1q:
C. elegans INX-6 gap junction hemichannel
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-9571, PDB-5h1r:
C. elegans INX-6 gap junction channel
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • caenorhabditis elegans (invertebrata)
KeywordsTRANSPORT PROTEIN / innexin / gap junction channel / octamer / wild type

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