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Figure 2.
Figure 2. Solution structures of GroEL–ATP[7]–GroES and
GroEL–ADP[7]–GroES. (a) Surface representation of the
side view of the GroEL–ATP[7]–GroES complex. (b) Surface
representation of the side view of the GroEL–ADP[7]–GroES
complex. (c,d) Central sections through the cryo-EM maps are
shown as a semitransparent surface in either gold (c; ATP) or
blue (d; ADP), with the atomic coordinates for the GroEL
equatorial (green; residues 3–136 and 410–524), intermediate
(yellow; residues 137–191 and 374–409), apical (red;
residues 192–373, except for 353–361 at the tip of the
mobile helical hairpin in the trans ring) and GroES (magenta)
fitted in. The seven-fold axis of the GroEL–GroES oligomer is
vertical and in the image plane for all figures. The resolutions
of the ATP- and ADP-bound maps are 7.7 Å and 8.7 Å,
respectively, determined by Fourier shell correlation at a
cutoff of 0.5. Fourier shell correlation curves for both
reconstructions are shown in Supplementary Figure 1.
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