5H1Q

C. elegans INX-6 gap junction hemichannel

Summary for 5H1Q

• Entry DOI: 10.2210/pdb5h1q/pdb
• Related: 5H1R
• EMDB information: 9570
• Descriptor: Innexin-6 (1 entity in total)
• Functional Keywords: innexin, gap junction channel, octamer, wild type, transport protein
• Biological source: Caenorhabditis elegans
• Cellular location: Cell membrane ; Multi-pass membrane protein : Q9U3N4
• Total number of polymer chains: 8
• Total formula weight: 361390.13

Authors

Oshima, A.,Tani, K.,Fujiyoshi, Y. (deposition date: 2016-10-11, release date: 2016-12-07, Last modification date: 2025-06-25)

Primary citation

Oshima, A.,Tani, K.,Fujiyoshi, Y.
Atomic structure of the innexin-6 gap junction channel determined by cryo-EM
Nat Commun, 7:13681-13681, 2016

PubMed 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 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.

PubMed: 27905396
DOI: 10.1038/ncomms13681

Experimental method

ELECTRON MICROSCOPY (3.3 Å)