Figure 4. The K372-E380 salt bridge is not required for either nucleotide binding or hydrolysis. (A) 1 µM of the purified cytoplasmic domains (ATL2 1–467) of the indicated proteins were incubated with 5 µM (circles), 10 µM (squares), or 20 µM (triangles) GTP and assayed for phosphate release at the indicated times. Each point represents the means of two independent measurements. (B) A Lineweaver–Burk plot based on initial velocities from A was used to extract the KM of the indicated ATL2 proteins for GTP. (C) The indicated concentrations of wild-type ATL2 were incubated with 0.2 mM GTP followed by assaying for phosphate release. (D) 0.3, 0.6, or 1.25 µM of the indicated ATL2 variants was incubated with 0.2 mM GTP followed by an assay for phosphate release. Values represent the means of three independent measurements ± SD. v, initial velocity.
Figure 4.

The K372-E380 salt bridge is not required for either nucleotide binding or hydrolysis. (A) 1 µM of the purified cytoplasmic domains (ATL2 1–467) of the indicated proteins were incubated with 5 µM (circles), 10 µM (squares), or 20 µM (triangles) GTP and assayed for phosphate release at the indicated times. Each point represents the means of two independent measurements. (B) A Lineweaver–Burk plot based on initial velocities from A was used to extract the KM of the indicated ATL2 proteins for GTP. (C) The indicated concentrations of wild-type ATL2 were incubated with 0.2 mM GTP followed by assaying for phosphate release. (D) 0.3, 0.6, or 1.25 µM of the indicated ATL2 variants was incubated with 0.2 mM GTP followed by an assay for phosphate release. Values represent the means of three independent measurements ± SD. v, initial velocity.

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