7y46
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7y46]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Squalus_acanthias Squalus acanthias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y46 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7y46]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Squalus_acanthias Squalus acanthias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Y46 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Y46 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 7.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCW:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE'>PCW</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=7y46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y46 OCA], [https://pdbe.org/7y46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y46 RCSB], [https://www.ebi.ac.uk/pdbsum/7y46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y46 ProSAT]</span></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=7y46 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7y46 OCA], [https://pdbe.org/7y46 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7y46 RCSB], [https://www.ebi.ac.uk/pdbsum/7y46 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7y46 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/C4IX13_SQUAC C4IX13_SQUAC] 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.[RuleBase:RU004369] | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Na(+) ,K(+) -ATPase (NKA) is one of the most important members of the P-type ion-translocating ATPases and plays a pivotal role in establishing electrochemical gradients for Na(+) and K(+) across the cell membrane. Presented here is a 3.3 A resolution structure of NKA in the E2.2K(+) state solved by cryo-electron microscopy. It is a stable state with two occluded K(+) after transferring three Na(+) into the extracellular medium and releasing inorganic phosphate bound to the cytoplasmic P domain. We describe how the extracellular ion pathway wide open in the E2P state becomes closed and locked in E2.2K(+) , linked to events at the phosphorylation site more than 50 A away. We also show, although at low resolution, how ATP binding to NKA in E2.2K(+) relaxes the gating machinery and thereby accelerates the transition into the next step, that is, the release of K(+) into the cytoplasm, more than 100 times. | ||
| + | |||
| + | Cryo-electron microscopy of Na(+) ,K(+) -ATPase reveals how the extracellular gate locks in the E2.2K(+) state.,Kanai R, Cornelius F, Vilsen B, Toyoshima C FEBS Lett. 2022 Oct;596(19):2513-2524. doi: 10.1002/1873-3468.14437. Epub 2022 , Jul 6. PMID:35747985<ref>PMID:35747985</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7y46" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[ATPase 3D structures|ATPase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Cryo-EM structure of the Na+,K+-ATPase in the E2.2K+ state after addition of ATP
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