Fig. 2.

Native mass spectrometry reveals individual lipid-binding events can allosteric modulate the interaction between GlnK and AmtB. a Representative mass spectrum of AmtB–GlnK at 2 μM in buffer containing 50 µM ADP and 20 µM 1,1′,2,2′-tetraoleoyl-cardiolipin (TOCDL). b Plot of equilibrium dissociation constants (K _D) for GlnK binding to either apo AmtB or AmtB bound to phosphatidylethanolamine (PE), phosphatidylglycerol (PG), phosphatidylserine (PS), and phosphatidic acid (PA) containing 1-palmitoyl-2-oleoyl (PO, 16:0−18:1) tails, and TOCDL at 298 K (see Supplementary Fig. 7 for K _D abbreviations). Reported are the average and s.e.m. from repeated measurements (n = 3)