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. Author manuscript; available in PMC: 2014 Apr 2.
Published in final edited form as: Structure. 2013 Mar 7;21(4):540–549. doi: 10.1016/j.str.2013.01.017

Figure 4. The ATP binding sites in the closed form.

Figure 4

(A and B) The ATP sites of the CCT8-Q and CCT4-D subunits show the ADP-beryllium fluoride analogues (Be-yellow; F-magenta; Mg-green). The density corresponding to the adenosine and ribose moieties is well resolved in all subunits. Side-chains are labeled according to the position indices in the conservation analysis. The density is averaged over the four rings and contoured at 3σ.

(C) The evolutionary conservation of paralogous positions lining the ATP pockets in the eight subunits. The CCT8-Q subunit shows the most variation around the ATP site compared to the other seven subunits. Positions that are identical for at least 10 of the 13 tested eukaryotic species are marked by a capital letter. Positions that are identical for at least 7 of the 13 species are marked by a lowercase letter and less conserved positions are marked by a star. High Entropy Ratio (see Methods) marks signature positions that are highly conserved across species but differ between subunit types.