8d3v: Difference between revisions
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The entry | ==Human alpha3 Na+/K+-ATPase in its cytoplasmic side-open state== | ||
<StructureSection load='8d3v' size='340' side='right'caption='[[8d3v]], [[Resolution|resolution]] 3.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8d3v]] 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=8D3V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8D3V FirstGlance]. <br> | |||
</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=8d3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8d3v OCA], [https://pdbe.org/8d3v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8d3v RCSB], [https://www.ebi.ac.uk/pdbsum/8d3v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8d3v ProSAT]</span></td></tr> | |||
</table> | |||
== Disease == | |||
[[https://www.uniprot.org/uniprot/AT1A3_HUMAN AT1A3_HUMAN]] Rapid-onset dystonia-parkinsonism;Alternating hemiplegia of childhood;Non-specific early-onset epileptic encephalopathy;Cerebellar ataxia-areflexia-pes cavus-optic atrophy-sensorineural hearing loss syndrome. 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-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 8d3v" 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 cytoplasmic side-open stateHuman alpha3 Na+/K+-ATPase in its cytoplasmic side-open state
Structural highlights
Disease[AT1A3_HUMAN] Rapid-onset dystonia-parkinsonism;Alternating hemiplegia of childhood;Non-specific early-onset epileptic encephalopathy;Cerebellar ataxia-areflexia-pes cavus-optic atrophy-sensorineural hearing loss syndrome. 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[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.[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-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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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