Research Article

Basal Glutathionylation of Na,K-ATPase α-Subunit Depends on Redox Status of Cells during the Enzyme Biosynthesis

Table 4

Cysteine residues with unresolved GSH-like electron density and effect of their substitution by alanine or serine on Na,K-ATPase activity.

PDB ID/Cys position3WGU3WGV3KDP4HYT3B8ENa,K-ATPase activity according to [24],
mutant/wild type, %

204Density Density Small density Small density Small density49.2
242

367Density Fragmented density Distant density nd nd23.4
69822.9

452Density Fragmented density Density Fragmented density Density 25.3
456

599Density Fragmented densityDensity Fragmented DensityDensity43.5

Abbreviations and all other details are given in the legend of Table 2.
Cells with Cys 242 Ala or Cys 242 Ser mutant of Na,K-ATPase did not survive under ouabain selective pressure.
Activity of Cys 452, Cys 456, and Cys 457 Ser mutant of Na,K-ATPase.