Fig. 6: ATPase activity and structure of the PspA dL10 mutant.
From: Structural plasticity of bacterial ESCRT-III protein PspA in higher-order assemblies
a, Schematic secondary structure topology of the PspA monomer (α1, red; α2 + 3, violet; α4, blue; α5, cyan). The deletion of loop residues 156–165 (dL10) and relevant mutations are indicated in green. b, ATPase activity of PspA WT and dL10 measured by a malachite-green-based assay. The boxplots show the mean ± s.e.m. as boxes, the 10–90th percentile as whiskers and outliers as diamonds. P values of two-sample t-test: WT versus dL10, P = 3.92 × 10−10; WT, n = 39, dL10, n = 23. For all measurements, samples of at least three biological replicates were included c, Histogram of rod diameters and the normalized abundance of PspA dL10 rods (green), PspA dL10 rods in the presence of ATP (yellow) and PspA WT rods (gray) for comparison. PspA dL10 has a narrow diameter distribution that is not affected by ATP addition. d,e, The associated cryo-EM structures of PspA dL10 (d) and PspA dL10 + ATP (e) are shown in cross-sectional top and side views. f, Left, comparison of the cryo-EM density maps of PspA + ATP (gray) and PspA dL10 (green). Red arrowheads indicate the additional density for the loop that is missing in the dL10 map. Right, cryo-EM density map of PspA dL10 with the PspA WT model.
