8d3x | pdb_00008d3x

Human alpha3 Na+/K+-ATPase in its K+-occluded state

spinqualitylabelsall models 8d3x, resolution 4.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8d3x is a 3 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.1Å Ligands: MF4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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). Involved in cell adhesion and establishing epithelial cell polarity. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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