7dsc: Difference between revisions
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==CALHM1 open state with disordered CTH== | |||
<StructureSection load='7dsc' size='340' side='right'caption='[[7dsc]], [[Resolution|resolution]] 3.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7dsc]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DSC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DSC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=7dsc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dsc OCA], [https://pdbe.org/7dsc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dsc RCSB], [https://www.ebi.ac.uk/pdbsum/7dsc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dsc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/E7F2J4_DANRE E7F2J4_DANRE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Calcium homeostasis modulator 1 (CALHM1) is a voltage- and Ca(2+)-gated ATP channel that plays an important role in neuronal signaling. However, as the previously reported CALHM structures are all in the ATP-conducting state, the gating mechanism of ATP permeation is still elusive. Here, we report cryo-EM reconstructions of two Danio rerio CALHM1 heptamers with ordered or flexible long C-terminal helices at resolutions of 3.2 A and 2.9 A, respectively, and one D. rerio CALHM1 octamer with flexible long C-terminal helices at a resolution of 3.5 A. Structural analysis shows that the heptameric CALHM1s are in an ATP-nonconducting state with a central pore diameter of approximately 6.6 A. Compared with those inside the octameric CALHM1, the N-helix inside the heptameric CALHM1 is in the "down" position to avoid steric clashing with the adjacent TM1 helix. Molecular dynamics simulations show that as the N-helix moves from the "down" position to the "up" position, the pore size of ATP molecule permeation increases significantly. Our results provide important information for elucidating the mechanism of ATP molecule permeation in the CALHM1 channel. | |||
Cryo-EM structure of the heptameric calcium homeostasis modulator 1 channel.,Ren Y, Li Y, Wang Y, Wen T, Lu X, Chang S, Zhang X, Shen Y, Yang X J Biol Chem. 2022 May;298(5):101838. doi: 10.1016/j.jbc.2022.101838. Epub 2022 , Mar 24. PMID:35339491<ref>PMID:35339491</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7dsc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Danio rerio]] | |||
[[Category: Large Structures]] | |||
[[Category: Ren Y]] | |||
[[Category: Shen YQ]] | |||
[[Category: Yang X]] | |||
Latest revision as of 09:52, 25 January 2023
CALHM1 open state with disordered CTHCALHM1 open state with disordered CTH
Structural highlights
FunctionPublication Abstract from PubMedCalcium homeostasis modulator 1 (CALHM1) is a voltage- and Ca(2+)-gated ATP channel that plays an important role in neuronal signaling. However, as the previously reported CALHM structures are all in the ATP-conducting state, the gating mechanism of ATP permeation is still elusive. Here, we report cryo-EM reconstructions of two Danio rerio CALHM1 heptamers with ordered or flexible long C-terminal helices at resolutions of 3.2 A and 2.9 A, respectively, and one D. rerio CALHM1 octamer with flexible long C-terminal helices at a resolution of 3.5 A. Structural analysis shows that the heptameric CALHM1s are in an ATP-nonconducting state with a central pore diameter of approximately 6.6 A. Compared with those inside the octameric CALHM1, the N-helix inside the heptameric CALHM1 is in the "down" position to avoid steric clashing with the adjacent TM1 helix. Molecular dynamics simulations show that as the N-helix moves from the "down" position to the "up" position, the pore size of ATP molecule permeation increases significantly. Our results provide important information for elucidating the mechanism of ATP molecule permeation in the CALHM1 channel. Cryo-EM structure of the heptameric calcium homeostasis modulator 1 channel.,Ren Y, Li Y, Wang Y, Wen T, Lu X, Chang S, Zhang X, Shen Y, Yang X J Biol Chem. 2022 May;298(5):101838. doi: 10.1016/j.jbc.2022.101838. Epub 2022 , Mar 24. PMID:35339491[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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