- PDB-5h1q: C. elegans INX-6 gap junction hemichannel -
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Basic information
Entry
Database: PDB / ID: 5h1q
Title
C. elegans INX-6 gap junction hemichannel
Components
Innexin-6
Keywords
TRANSPORT PROTEIN / innexin / gap junction channel / octamer / wild type
Function / homology
gap junction hemi-channel activity / Innexin / Innexin / Pannexin family profile. / gap junction / gap junction channel activity / monoatomic ion transmembrane transport / plasma membrane / Innexin-6
Function and homology information
Biological species
Caenorhabditis elegans (invertebrata)
Method
ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.3 Å
Journal: Nat Commun / Year: 2016 Title: Atomic structure of the innexin-6 gap junction channel determined by cryo-EM. Authors: Atsunori Oshima / Kazutoshi Tani / Yoshinori Fujiyoshi / Abstract: 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 ...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.
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