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1.
Figure 2

Figure 2. From: INSIGHTS INTO THE INTRA-RING SUBUNIT ORDER OF TRIC/CCT: A STRUCTURAL AND EVOLUTIONARY ANALYSIS.

Two complementary residues at the interface of two thermosome subunits. Unit α (blue) and subunit β (red) are the left and right subunits, respectively, in the top ring when viewed from the side of the particle. In TRiC this salt bridge is not conserved between all subunits. The amino acids at these two positions in different organisms are shown in Table 1.

Nir Kalisman, et al. Pac Symp Biocomput. :252-259.
2.
Figure 3

Figure 3. From: INSIGHTS INTO THE INTRA-RING SUBUNIT ORDER OF TRIC/CCT: A STRUCTURAL AND EVOLUTIONARY ANALYSIS.

Three complementary residues at the interface between two thermosome subunits. Subunit α (blue) and subunit β (red) are the left and right subunits, respectively, in the top ring when viewed from the side of the particle. The amino acids at these three positions in different organisms are shown in Table 2.

Nir Kalisman, et al. Pac Symp Biocomput. :252-259.
3.
Figure 1

Figure 1. From: INSIGHTS INTO THE INTRA-RING SUBUNIT ORDER OF TRIC/CCT: A STRUCTURAL AND EVOLUTIONARY ANALYSIS.

Our structural model is based on the known structure of the thermosome (PDB file 1A6D), which has α (blue) and β (red) subunits that alternate around each of the two rings. The structure is viewed from the top (left) and side (right). The three domains of one of the α subunits in the top ring are colored cyan, green & magenta for the equatorial, middle & apical domains, respectively. The central schematic shows how to map the 8 subunits - A, B, G, D, E, H, Q & Z - of TRiC in a proposed arrangement (boxed) onto the top ring of the thermosome. This arrangement is brought as an example only, and is not part of our suggested set of 72.

Nir Kalisman, et al. Pac Symp Biocomput. :252-259.

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