7y45

Cryo-EM structure of the Na+,K+-ATPase in the E2.2K+ state

spinqualitylabelsall models 7y45, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7y45 is a 6 chain structure with sequence from Squalus acanthias. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.3Å Ligands: BMA, CLR, FUC, K, MAN, NAG, PCW Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q70Q12_SQUAC 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase 3D structures

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