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Figure 9.
Figure 9 Electrostatic surface potentials of HslV and HslU.
Positions of some amino-acid residues are labeled in each
figure. (a) View looking down the sixfold axis of the HslV
dodecamer from the HslUV complex (Sousa et al., 2000[Sousa, M.
C., Trame, C. B., Tsuruta, H., Wilbanks, S. M., Reddy, V. S. &
McKay, D. B. (2000). Cell, 103, 633-643.]). Arrows indicate the
electropositive grooves into which the carboxy-terminal helices
of HslU intercalate. (b) Carboxy-terminal helix of one protomer
of HslU in its conformation from the HslUV complex. (c) Side
view showing the interface between the carboxy-terminal helix of
HslU, shown as a ball-and-stick model, and the groove between
two HslV protomers. Electrostatic potentials were computed with
the program GRASP (Nicholls & Honig, 1991[Nicholls, A. & Honig,
B. J. (1991). J. Comput. Chem. 12, 435-445.]), using a
dielectric constant of 2.0 for the interior of the protein and
80.0 for the solvent area and an effective ionic strength
equivalent to 1.0 M salt.
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