Extended Data Fig. 2: ATPase activity of AtABCG16.
From: Cryo-EM structure and molecular mechanism of the jasmonic acid transporter ABCG16
a-b, ATPase activity of AtABCG16 purified in buffer containing 0.05% digitonin (n = 4) (a) and 0.01% LMNG + 0.001% CHS + 0.0033% GDN (n = 3 for protein incubate with 0.6, 1.0 and 6.0 mM ATP; n = 4 for protein incubate with 0.1, 0.2, 0.4, 1.5, 2.0, 3.0, 4.0 and 5.0 mM ATP) (b). c-f, Effect of substrate addition on the ATPase activity of AtABCG16 purified in buffer containing 0.05% digitonin (n = 3 for protein incubate with 12.5 μM JA; n = 4 for protein incubate with 3, 6, 25, 50, 125 μM JA.) (c), 0.01% LMNG + 0.001% CHS + 0.0033% GDN (n = 3) (d), and reconstituted in nanodiscs (n = 3) (e) and liposomes (n = 3) (f). Error bars are mean ± s.e.m.
