Cryo-EM structure of non gastric H,K-ATPase alpha2 mutants
Ontology highlight
ABSTRACT:
SUBMITTER: Kazuhiro Abe
PROVIDER: EMPIAR-11248 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structure and function of H<sup>+</sup>/K<sup>+</sup> pump mutants reveal Na<sup>+</sup>/K<sup>+</sup> pump mechanisms.
Young Victoria C VC Nakanishi Hanayo H Meyer Dylan J DJ Nishizawa Tomohiro T Oshima Atsunori A Artigas Pablo P Abe Kazuhiro K
Nature communications 20220909 1
Ion-transport mechanisms evolve by changing ion-selectivity, such as switching from Na<sup>+</sup> to H<sup>+</sup> selectivity in secondary-active transporters or P-type-ATPases. Here we study primary-active transport via P-type ATPases using functional and structural analyses to demonstrate that four simultaneous residue substitutions transform the non-gastric H<sup>+</sup>/K<sup>+</sup> pump, a strict H<sup>+</sup>-dependent electroneutral P-type ATPase, into a bona fide Na<sup>+</sup>-depend ...[more]
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