Specific Sites in the Cytoplasmic N Terminus Modulate Conformational Transitions of the Na,K-ATPase (original) (raw)

The cytoplasmic N terminus of the Na,K-ATPase plays a critical role in modulating the enzyme's conformational transitions, specifically in the equilibrium between the E1 and E2 states. Through a clustered charge-to-alanine mutagenesis approach, this study identifies key residues within two helical regions, H1 and H2, that impact the stability of these states. Notably, alanine substitutions at positions 31KKE in H1 and 47HRK in H2 demonstrate distinct functions in stabilizing the E2P and E2 states, contributing valuable insights into the mechanisms underlying Na,K-ATPase catalysis.