Molecular Structure of the Na+,K+-ATPase α4β1 Isoform in Its Ouabain-Bound Conformation
Kazuhiro Abe, Jeff McDermott, Hridya Valia Madapally, Parthiban Marimuthu, Chai C Gopalasingam, Christoph Gerle, Hideki Shigematsu, Himanshu Khandelia, Gustavo Blanco, Olga V Fedorova · 2024
Read Molecular Structure of the Na+,K+-ATPase α4β1 Isoform in Its Ouabain-Bound Conformation by Kazuhiro Abe, Jeff McDermott, Hridya Valia Madapally, Parthiban Marimuthu, Chai C Gopalasingam, Christoph Gerle, Hideki Shigematsu, Himanshu Khandelia, Gustavo Blanco, Olga V Fedorova (2024) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-11594824.txt.
Description
The sodium-potassium pump keeps every animal cell's electrical balance, and one special version of it exists only in sperm. Kazuhiro Abe and co-authors solve that version's structure in a 2024 paper. The isoform, built from alpha4 and beta1 subunits, sits in the sperm's tail and drives the swimming that fertility depends on.
Using cryo-electron microscopy, the team captured the pump holding ouabain, a plant toxin that jams such pumps, at near-atomic resolution. The overall shape matches the common isoform, but the ouabain pocket and other spots differ in step with its unique sequence. Simulations also found a docking site for fatty sugar molecules that may tune the pump's behavior. The structure explains how this sperm-only machine differs from its household cousins.
Catalog record
| CREATOR | Kazuhiro Abe, Jeff McDermott, Hridya Valia Madapally, Parthiban Marimuthu, Chai C Gopalasingam, Christoph Gerle, Hideki Shigematsu, Himanshu Khandelia, Gustavo Blanco, Olga V Fedorova |
|---|---|
| YEAR | 2024 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 32 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |