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Figure 4.
Figure 4. J Domain-Induced Changes in Linker Conformation May
Activate ATPase through Interactions with Y371 and I181
(A)
Structures of the J domain (cyan) and Hsc70 residues 371–389,
181, and 187 with the linker in the “Out” conformation.
Hsc70 linker residues 383–389 and 371–382+181+187 are in
magenta and green, respectively. The ED around the illustrated
Hsc70 residues is contoured at 0.5 σ.
(B) As in (A), but
with the linker in the “In” conformation and extending to
residue 390; average B factors for linker residues 383–389
(“Out”) or 383–390 (“In”) are 55 and 56, respectively,
whereas the average B factor for residues 3–382 of the NBD is
28.
(C) Effects of J domain on the ATPase rates of WT and
mutant Hsc70ΔC enzymes. Experimental conditions as in Figure 1,
but with Hsc70ΔC and J domain (+J) at 10 and 25 μM,
respectively. Error bars are ± SEM for n = 3.
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