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TitleCryo-EM structures of undocked innexin-6 hemichannels in phospholipids.
Journal, issue, pagesSci Adv, Vol. 6, Issue 7, Page eaax3157, Year 2020
Publish dateFeb 12, 2020
AuthorsBatuujin Burendei / Ruriko Shinozaki / Masakatsu Watanabe / Tohru Terada / Kazutoshi Tani / Yoshinori Fujiyoshi / Atsunori Oshima /
PubMed AbstractGap junctions form intercellular conduits with a large pore size whose closed and open states regulate communication between adjacent cells. The structural basis of the mechanism by which gap ...Gap junctions form intercellular conduits with a large pore size whose closed and open states regulate communication between adjacent cells. The structural basis of the mechanism by which gap junctions close, however, remains uncertain. Here, we show the cryo-electron microscopy structures of innexin-6 (INX-6) gap junction proteins in an undocked hemichannel form. In the nanodisc-reconstituted structure of the wild-type INX-6 hemichannel, flat double-layer densities obstruct the channel pore. Comparison of the hemichannel structures of a wild-type INX-6 in detergent and nanodisc-reconstituted amino-terminal deletion mutant reveals that lipid-mediated amino-terminal rearrangement and pore obstruction occur upon nanodisc reconstitution. Together with molecular dynamics simulations and electrophysiology functional assays, our results provide insight into the closure of the INX-6 hemichannel in a lipid bilayer before docking of two hemichannels.
External linksSci Adv / PubMed:32095518 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 3.8 Å
Structure data

9971

6kff

EMDB-9971, PDB-6kff:
Undocked INX-6 hemichannel in a nanodisc
Method: EM (single particle) / Resolution: 3.8 Å

9972

6kfg

EMDB-9972, PDB-6kfg:
Undocked INX-6 hemichannel in detergent
Method: EM (single particle) / Resolution: 3.8 Å

9973

6kfh

EMDB-9973, PDB-6kfh:
Undocked hemichannel of an N-terminal deletion mutant of INX-6 in a nanodisc
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • caenorhabditis elegans (invertebrata)
KeywordsTRANSPORT PROTEIN / Gap junctions / Innexin

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