Fig. 3: TRiC–actin–cochaperone complex. | Nature Structural & Molecular Biology

Fig. 3: TRiC–actin–cochaperone complex.

From: Snapshots of actin and tubulin folding inside the TRiC chaperonin

Fig. 3

a, Side slice map of closed TRiC, showing protein density in both chamber cavities. b, Top-down view of actin model modeled from map density (gray), colored by subdomains. c, Top-down view of chamber interior showing TRiC subunits in contact with actin (yellow). Top inset, three subunits form main contacts with actin (gray). Bottom inset, subunit side chains (sticks) in contact with actin (yellow). d, Overlay of our actin model with native actin structure (PDB 6RSW). e, Non-TRiC map density at lower threshold that can accommodate actin (yellow) bound with PhLP2A (gray). f, Overall model of TRiC–actin–PhLP2A ternary complex. PhLP2A helix H2 is not modeled and is shown as a cartoon cylinder.

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