Fig. 1: Interplay of ADP and Sub in the inhibition and stimulation of PCAT1 ATP turnover activity. | Nature Communications

Fig. 1: Interplay of ADP and Sub in the inhibition and stimulation of PCAT1 ATP turnover activity.

From: Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling

Fig. 1

A Sub stimulates ATP hydrolysis whereas ADP competitively inhibits it (see Supplementary Table 1). Sub partly reverses the inhibition of ADP. PCAT1 turnover data is the average of 15 repeats from 8 biological repeats. PCAT1 inhibition with 2 mM ADP with 5 mM Vi is the average of 4 technical from 2 biological repeats. Turnover data with 5× Sub is derived from 5 biological repeats. B Biphasic shape of ATP turnover determined under 10 mM Mg2+ curve suggests partial inhibition by free Mg2+. The data is the average from at least 2 biological repeats. C Multiphasic dependence of Vmax on the Mg2+ to ATP ratio. The data is the average of at least two biological repeats. All data are presented as mean values ± standard deviation.

Back to article page