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Cyo-EM structure of wildtype non-gastric proton pump in the presence of Na+, AlF and ADP

ABSTRACT:

SUBMITTER: Kazuhiro Abe

PROVIDER: EMPIAR-11722 | biostudies-other |

REPOSITORIES: biostudies-other

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An unusual conformation from Na+-sensitive non-gastric proton pump mutants reveals molecular mechanisms of cooperative Na+-binding.

Abe Kazuhiro K Nishizawa Tomohiro T Artigas Pablo P

Biochimica et biophysica acta. Molecular cell research 20230722 7

The Na+,K+-ATPase (NKA) and non-gastric H+,K+- ATPase (ngHKA) share ~65 % sequence identity, and nearly identical catalytic cycles. These pumps alternate between inward-facing (E1) and outward-facing (E2) conformations and differ in their exported substrate (Na+ or H+) and stoichiometries (3 Na+:2 K+ or 1 H+:1 K+). We reported that structures of the NKA-mimetic ngHKA mutant K794S/A797P/W ...[more]

PMID: 37482134

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