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| | <SX load='6kfh' size='340' side='right' viewer='molstar' caption='[[6kfh]], [[Resolution|resolution]] 3.60Å' scene=''> | | <SX load='6kfh' size='340' side='right' viewer='molstar' caption='[[6kfh]], [[Resolution|resolution]] 3.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6kfh]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KFH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6KFH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6kfh]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KFH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KFH FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">inx-6, opu-6, C36H8.2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.6Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6kfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kfh OCA], [http://pdbe.org/6kfh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kfh RCSB], [http://www.ebi.ac.uk/pdbsum/6kfh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kfh ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6kfh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kfh OCA], [https://pdbe.org/6kfh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kfh RCSB], [https://www.ebi.ac.uk/pdbsum/6kfh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kfh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/INX6_CAEEL INX6_CAEEL]] Structural component of the gap junctions.[UniProtKB:O61715] | + | [https://www.uniprot.org/uniprot/INX6_CAEEL INX6_CAEEL] Structural component of the gap junctions.[UniProtKB:O61715] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Caeel]] | + | [[Category: Caenorhabditis elegans]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Burendei, B]] | + | [[Category: Burendei B]] |
| - | [[Category: Fujiyoshi, Y]] | + | [[Category: Fujiyoshi Y]] |
| - | [[Category: Oshima, A]] | + | [[Category: Oshima A]] |
| - | [[Category: Shinozaki, R]] | + | [[Category: Shinozaki R]] |
| - | [[Category: Tani, K]] | + | [[Category: Tani K]] |
| - | [[Category: Terada, T]] | + | [[Category: Terada T]] |
| - | [[Category: Watanabe, M]] | + | [[Category: Watanabe M]] |
| - | [[Category: Gap junction]]
| + | |
| - | [[Category: Innexin]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
INX6_CAEEL Structural component of the gap junctions.[UniProtKB:O61715]
Publication Abstract from PubMed
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 Caenorhabditis elegans 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.
Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids.,Burendei B, Shinozaki R, Watanabe M, Terada T, Tani K, Fujiyoshi Y, Oshima A Sci Adv. 2020 Feb 12;6(7):eaax3157. doi: 10.1126/sciadv.aax3157. eCollection 2020, Feb. PMID:32095518[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burendei B, Shinozaki R, Watanabe M, Terada T, Tani K, Fujiyoshi Y, Oshima A. Cryo-EM structures of undocked innexin-6 hemichannels in phospholipids. Sci Adv. 2020 Feb 12;6(7):eaax3157. doi: 10.1126/sciadv.aax3157. eCollection 2020, Feb. PMID:32095518 doi:http://dx.doi.org/10.1126/sciadv.aax3157
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