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

MANGIALAVORI I, MONTES MR, ROSSI RC, FEDOSOVA NU, ROSSI JP.

FEBS LETTERS

ELSEVIER SCIENCE BV

Año: 2011 vol. 585 p. 1153 - 1157

0014-5793

Annular lipid–protein stoichiometry in native pig kidney Na+/K+-ATPase preparation was studied by[125I]TID-PC/16 labeling. Our data indicate that the transmembrane domain of the Na+/K+-ATPase inthe E1 state is less exposed to the lipids than in E2, i.e. the conformational transitions are accompaniedby 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 (a subunit) and 5.0 ± 0.4 (b subunit) in the E1 conformationand 32 ± 2 (a subunit) and 7 ± 1 (b subunit) in the E2 conformation.