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==Cryo-EM structure of the CALHM chimeric construct (9-mer)== | ==Cryo-EM structure of the CALHM chimeric construct (9-mer)== | ||
<StructureSection load='6lmx' size='340' side='right'caption='[[6lmx]]' scene=''> | <StructureSection load='6lmx' size='340' side='right'caption='[[6lmx]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LMX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LMX FirstGlance]. <br> | <table><tr><td colspan='2'>[[6lmx]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Japanese_killifish Japanese killifish]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6LMX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6LMX FirstGlance]. <br> | ||
</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=6lmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lmx OCA], [http://pdbe.org/6lmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lmx RCSB], [http://www.ebi.ac.uk/pdbsum/6lmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lmx ProSAT]</span></td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CALHM2, FAM26B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=8090 Japanese killifish])</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=6lmx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6lmx OCA], [http://pdbe.org/6lmx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6lmx RCSB], [http://www.ebi.ac.uk/pdbsum/6lmx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6lmx ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Calcium homeostasis modulator (CALHM) family proteins are Ca(2+)-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we present the cryo-electron microscopy (EM) structures of killifish CALHM1, human CALHM2, and Caenorhabditis elegans CLHM-1 at resolutions of 2.66, 3.4, and 3.6 A, respectively. The CALHM1 octamer structure reveals that the N-terminal helix forms the constriction site at the channel pore in the open state and modulates the ATP conductance. The CALHM2 undecamer and CLHM-1 nonamer structures show the different oligomeric stoichiometries among CALHM homologs. We further report the cryo-EM structures of the chimeric construct, revealing that the intersubunit interactions at the transmembrane domain (TMD) and the TMD-intracellular domain linker define the oligomeric stoichiometry. These findings advance our understanding of the ATP conduction and oligomerization mechanisms of CALHM channels. | |||
Cryo-EM structures of calcium homeostasis modulator channels in diverse oligomeric assemblies.,Demura K, Kusakizako T, Shihoya W, Hiraizumi M, Nomura K, Shimada H, Yamashita K, Nishizawa T, Taruno A, Nureki O Sci Adv. 2020 Jul 17;6(29):eaba8105. doi: 10.1126/sciadv.aba8105. eCollection, 2020 Jul. PMID:32832629<ref>PMID:32832629</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6lmx" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Japanese killifish]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Demura K]] | [[Category: Demura, K]] | ||
[[Category: Hiraizumi M]] | [[Category: Hiraizumi, M]] | ||
[[Category: Kusakizako T]] | [[Category: Kusakizako, T]] | ||
[[Category: Nishizawa T]] | [[Category: Nishizawa, T]] | ||
[[Category: Nureki O]] | [[Category: Nureki, O]] | ||
[[Category: Shihoya W]] | [[Category: Shihoya, W]] | ||
[[Category: Shimada H]] | [[Category: Shimada, H]] | ||
[[Category: Yamashita K]] | [[Category: Yamashita, K]] | ||
[[Category: Channel]] | |||
[[Category: Membrane protein]] | |||
Revision as of 12:49, 9 September 2020
Cryo-EM structure of the CALHM chimeric construct (9-mer)Cryo-EM structure of the CALHM chimeric construct (9-mer)
Structural highlights
Publication Abstract from PubMedCalcium homeostasis modulator (CALHM) family proteins are Ca(2+)-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we present the cryo-electron microscopy (EM) structures of killifish CALHM1, human CALHM2, and Caenorhabditis elegans CLHM-1 at resolutions of 2.66, 3.4, and 3.6 A, respectively. The CALHM1 octamer structure reveals that the N-terminal helix forms the constriction site at the channel pore in the open state and modulates the ATP conductance. The CALHM2 undecamer and CLHM-1 nonamer structures show the different oligomeric stoichiometries among CALHM homologs. We further report the cryo-EM structures of the chimeric construct, revealing that the intersubunit interactions at the transmembrane domain (TMD) and the TMD-intracellular domain linker define the oligomeric stoichiometry. These findings advance our understanding of the ATP conduction and oligomerization mechanisms of CALHM channels. Cryo-EM structures of calcium homeostasis modulator channels in diverse oligomeric assemblies.,Demura K, Kusakizako T, Shihoya W, Hiraizumi M, Nomura K, Shimada H, Yamashita K, Nishizawa T, Taruno A, Nureki O Sci Adv. 2020 Jul 17;6(29):eaba8105. doi: 10.1126/sciadv.aba8105. eCollection, 2020 Jul. PMID:32832629[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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