Fig. 1: Structure of TRiC–Nb18 complex.
From: Snapshots of actin and tubulin folding inside the TRiC chaperonin
a, A map at 2.5-Å resolution of closed-TRiC in complex with Nb18 in top (left) and side (right) views. b, Cartoon representation of closed TRiC in same views as in a. c, Flattened scheme of subunit arrangement for the two stacked rings. d, Nucleotide-binding site of CCT7 bound with ADP–Mg2+–AlF3. Conserved interacting residues are shown as sticks. e, Side slice of closed-TRiC (fully empty class 4), highlighting the septum at the ring interface that creates two cavities in the TRiC interior. f, Section of the ring interface, viewed from the interior, showing examples of intra-ring (termini–hairpin sheets) and inter-ring (plug–socket, N extensions) contacts.
