Computer modelling reveals new conformers of the ATP binding loop of Na⁺/K⁺-ATPase involved in the transphosphorylation process of the sodium pump.

ABSTRACT: Hydrolysis of ATP by Na⁺/K⁺-ATPase, a P-Type ATPase, catalyzing active Na⁺ and K⁺ transport through cellular membranes leads transiently to a phosphorylation of its catalytical α-subunit. Surprisingly, three-dimensional molecular structure analysis of P-type ATPases reveals that binding of ATP to the N-domain connected by a hinge to the P-domain is much too far away from the Asp³⁶⁹ to allow the transfer of ATP's terminal phosphate to its aspartyl-phosphorylation site. In order to get information for how the transfer of the γ-phosphate group of ATP to the Asp³⁶⁹ is achieved, analogous molecular modeling of the M₄-M₅ loop of ATPase was performed using the crystal data of Na⁺/K

SUBMITTER: Tejral G 

PROVIDER: S-EPMC5354106 | biostudies-literature | 2017

REPOSITORIES: biostudies-literature