8d3x: Difference between revisions
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==Human alpha3 Na+/K+-ATPase in its K+-occluded state== | |||
<StructureSection load='8d3x' size='340' side='right'caption='[[8d3x]], [[Resolution|resolution]] 4.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8d3x]] 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=8D3X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D3X FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MF4:TETRAFLUOROMAGNESATE(2-)'>MF4</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=8d3x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d3x OCA], [https://pdbe.org/8d3x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d3x RCSB], [https://www.ebi.ac.uk/pdbsum/8d3x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d3x ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[https://www.uniprot.org/uniprot/AT1B1_HUMAN AT1B1_HUMAN]] This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane (PubMed:19694409). Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1 (PubMed:34011520).<ref>PMID:19694409</ref> <ref>PMID:34011520</ref> Involved in cell adhesion and establishing epithelial cell polarity.<ref>PMID:19694409</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-AlF4(-) trapped Na(+)-occluded (E1*P-ADP), BeF3(-) trapped exoplasmic side-open (E2P) and MgF4(2-) trapped K(+)-occluded (E2*Pi) 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: | <div class="pdbe-citations 8d3x" style="background-color:#fffaf0;"></div> | ||
[[Category: Bai | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Bai X]] | |||
[[Category: Nguyen PT]] | |||
Revision as of 10:47, 21 September 2022
Human alpha3 Na+/K+-ATPase in its K+-occluded stateHuman alpha3 Na+/K+-ATPase in its K+-occluded state
Structural highlights
Function[AT1B1_HUMAN] This is the non-catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of Na(+) and K(+) ions across the plasma membrane. The beta subunit regulates, through assembly of alpha/beta heterodimers, the number of sodium pumps transported to the plasma membrane (PubMed:19694409). Plays a role in innate immunity by enhancing virus-triggered induction of interferons (IFNs) and interferon stimulated genes (ISGs). Mechanistically, enhances the ubiquitination of TRAF3 and TRAF6 as well as the phosphorylation of TAK1 and TBK1 (PubMed:34011520).[1] [2] Involved in cell adhesion and establishing epithelial cell polarity.[3] 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-AlF4(-) trapped Na(+)-occluded (E1*P-ADP), BeF3(-) trapped exoplasmic side-open (E2P) and MgF4(2-) trapped K(+)-occluded (E2*Pi) 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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