The Na⁺,K⁺-ATPase in complex with beryllium fluoride mimics an ATPase phosphorylated state.

ABSTRACT: The Na⁺,K⁺-ATPase generates electrochemical gradients of Na⁺ and K⁺ across the plasma membrane via a functional cycle that includes various phosphoenzyme intermediates. However, the structure and function of these intermediates and how metal fluorides mimick them require further investigation. Here, we describe a 4.0 Å resolution crystal structure and functional properties of the pig kidney Na⁺,K⁺-ATPase stabilized by the inhibitor beryllium fluoride (denoted E2-BeF_x). E2-BeF_x is expected to mimic properties of the E2P phosphoenzyme, yet with unknown characteristics of ion and ligand binding. The structure resembles the E2P form obtained by phosphorylation from inorganic phosphate (P_i) and st

SUBMITTER: Fruergaard MU 

PROVIDER: S-EPMC9485054 | biostudies-literature | 2022 Sep

REPOSITORIES: biostudies-literature