Dynamic lipid-protein stoichiometry on E-1 and E-2 conformations of the Na+/K+-ATPase

作者：Mangialavori Irene; Montes Monica R^*; Rossi Rolando C; Fedosova Natalya U; Rossi Jean Paul F C

来源：FEBS Letters, 2011, 585(8): 1153-1157.

DOI：10.1016/j.febslet.2011.03.024

• P-ATPase
• E-1-E-2 conformational transition
• Transmembrane segment
• Photolabeling procedure
• Annular lipid
• Na+/K+-ATPase

Annular lipid-protein stoichiometry in native pig kidney Na+/K+-ATPase preparation was studied by [I-125] TID-PC/16 labeling. Our data indicate that the transmembrane domain of the Na+/K+-ATPase in the E-1 state is less exposed to the lipids than in E-2, i.e. the conformational transitions are accompanied by changes in the number of annular lipids but not in the affinity of these lipids for the protein. The lipid-protein stoichiometry was 23 +/- 2 (alpha subunit) and 5.0 +/- 0.4 (beta subunit) in the E-1 conformation and 32 +/- 2 (alpha subunit) and 7 +/- 1 (beta subunit) in the E-2 conformation.

• 出版日期2011-4-20