Cryo‐electron microscopy of Na <sup>+</sup> ,K <sup>+</sup> ‐ <scp>ATPase</scp> reveals how the extracellular gate locks in the <scp>E2</scp> · <scp>2K</scp> <sup>+</sup> state-Reference-Cited by-同舟云学术

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Cryo‐electron microscopy of Na ⁺ ,K ⁺ ‐ ATPase reveals how the extracellular gate locks in the E2 · 2K ⁺ state

Published:2022-07-06 Issue:19 Volume:596 Page:2513-2524
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:FEBS Letters

Author:

Kanai Ryuta¹^ORCID,Cornelius Flemming²^ORCID,Vilsen Bente²^ORCID,Toyoshima Chikashi¹^ORCID

Affiliation:

1. Institute for Quantitative Biosciences The University of Tokyo Japan

2. Department of Biomedicine Aarhus University Denmark

Funder

Japan Society for the Promotion of Science

Lundbeckfonden

Novo Nordisk Fonden

Takeda Science Foundation

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.14437

Reference36 articles.

1. Finding Na,K‐ATPase: I – from cell to molecule;Apell H‐J;Substantia,2018

2. K‐ATPase II ‐ from fluxes to ion movements;Finding Apell H‐J.;Substantia,2019

3. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution

4. Structural similarities of Na,K-ATPase and SERCA, the Ca2+-ATPase of the sarcoplasmic reticulum

5. Crystal structure of a Na+-bound Na+,K+-ATPase preceding the E1P state

Cited by 3 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Crystal structures of Na⁺,K⁺‐ATPase reveal the mechanism that converts the K⁺‐bound form to Na⁺‐bound form and opens and closes the cytoplasmic gate;FEBS Letters;2023-07-06

2. Fast-forward on P-type ATPases: recent advances on structure and function;Biochemical Society Transactions;2023-06-02

3. Solid-state NMR chemical shift analysis for determining the conformation of ATP bound to Na,K-ATPase in its native membrane;RSC Advances;2023

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