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.
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| Method: | Electron Microscopy, Resolution 3.3Å |
| Ligands: | , , , , , , |
| 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kanai R, Cornelius F, Vilsen B, Toyoshima C. Cryo-electron microscopy of Na(+) ,K(+) -ATPase reveals how the extracellular gate locks in the E2·2K(+) state. FEBS Lett. 2022 Oct;596(19):2513-2524. PMID:35747985 doi:10.1002/1873-3468.14437
