8d3u: Difference between revisions
New page: '''Unreleased structure''' The entry 8d3u is ON HOLD Authors: Nguyen, P.T., Bai, X. Description: Human alpha3 Na+/K+-ATPase in its Na+-occluded state [[Category: Unreleased Structures]... |
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The entry | ==Human alpha3 Na+/K+-ATPase in its Na+-occluded state== | ||
<StructureSection load='8d3u' size='340' side='right'caption='[[8d3u]], [[Resolution|resolution]] 3.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8d3u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8D3U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D3U FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</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=8d3u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d3u OCA], [https://pdbe.org/8d3u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d3u RCSB], [https://www.ebi.ac.uk/pdbsum/8d3u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d3u ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[https://www.uniprot.org/uniprot/AT1A3_HUMAN AT1A3_HUMAN] Non-specific early-onset epileptic encephalopathy;Cerebellar ataxia-areflexia-pes cavus-optic atrophy-sensorineural hearing loss syndrome;Alternating hemiplegia of childhood;Rapid-onset dystonia-parkinsonism. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AT1A3_HUMAN AT1A3_HUMAN] This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.<ref>PMID:33880529</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
P2-type ATPase sodium-potassium pumps (Na(+)/K(+)-ATPases) are ion-transporting enzymes that use ATP to transport Na(+) and K(+) on opposite sides of the lipid bilayer against their electrochemical gradients to maintain ion concentration gradients across the membranes in all animal cells. Despite the available molecular architecture of the Na(+)/K(+)-ATPases, a complete molecular mechanism by which the Na(+) and K(+) ions access into and are released from the pump remains unknown. Here we report five cryo-electron microscopy (cryo-EM) structures of the human alpha3 Na(+)/K(+)-ATPase in its cytoplasmic side-open (E1), ATP-bound cytoplasmic side-open (E1*ATP), ADP-AlF(4)(-) trapped Na(+)-occluded (E1*P-ADP), BeF(3)(-) trapped exoplasmic side-open (E2P) and MgF(4)(2-) trapped K(+)-occluded (E2*P(i)) states. Our work reveals the atomically resolved structural detail of the cytoplasmic gating mechanism of the Na(+)/K(+)-ATPase. | |||
Structural basis for gating mechanism of the human sodium-potassium pump.,Nguyen PT, Deisl C, Fine M, Tippetts TS, Uchikawa E, Bai XC, Levine B Nat Commun. 2022 Sep 8;13(1):5293. doi: 10.1038/s41467-022-32990-x. PMID:36075933<ref>PMID:36075933</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Bai | <div class="pdbe-citations 8d3u" style="background-color:#fffaf0;"></div> | ||
[[Category: Nguyen | |||
==See Also== | |||
*[[ATPase 3D structures|ATPase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bai X]] | |||
[[Category: Nguyen PT]] | |||
Latest revision as of 17:27, 6 November 2024
Human alpha3 Na+/K+-ATPase in its Na+-occluded stateHuman alpha3 Na+/K+-ATPase in its Na+-occluded state
Structural highlights
DiseaseAT1A3_HUMAN Non-specific early-onset epileptic encephalopathy;Cerebellar ataxia-areflexia-pes cavus-optic atrophy-sensorineural hearing loss syndrome;Alternating hemiplegia of childhood;Rapid-onset dystonia-parkinsonism. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. FunctionAT1A3_HUMAN This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nutrients.[1] Publication Abstract from PubMedP2-type ATPase sodium-potassium pumps (Na(+)/K(+)-ATPases) are ion-transporting enzymes that use ATP to transport Na(+) and K(+) on opposite sides of the lipid bilayer against their electrochemical gradients to maintain ion concentration gradients across the membranes in all animal cells. Despite the available molecular architecture of the Na(+)/K(+)-ATPases, a complete molecular mechanism by which the Na(+) and K(+) ions access into and are released from the pump remains unknown. Here we report five cryo-electron microscopy (cryo-EM) structures of the human alpha3 Na(+)/K(+)-ATPase in its cytoplasmic side-open (E1), ATP-bound cytoplasmic side-open (E1*ATP), ADP-AlF(4)(-) trapped Na(+)-occluded (E1*P-ADP), BeF(3)(-) trapped exoplasmic side-open (E2P) and MgF(4)(2-) trapped K(+)-occluded (E2*P(i)) states. Our work reveals the atomically resolved structural detail of the cytoplasmic gating mechanism of the Na(+)/K(+)-ATPase. Structural basis for gating mechanism of the human sodium-potassium pump.,Nguyen PT, Deisl C, Fine M, Tippetts TS, Uchikawa E, Bai XC, Levine B Nat Commun. 2022 Sep 8;13(1):5293. doi: 10.1038/s41467-022-32990-x. PMID:36075933[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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