Figure 2: Structure of the tubulin-RB3-TTL-pironetin complex.
From: Pironetin reacts covalently with cysteine-316 of α-tubulin to destabilize microtubule
(a) Stereo views of experimental Fo–Fc difference electron density contoured at 3σ in green for pironetin and the side chains of C316 and K352 and the final refined 2Fo–Fc electron density contoured at 1σ in blue. The final refined positions of pironetin, C316 and K352 are shown in stick with carbons coloured cyan for pironetin and green for protein, oxygens red and nitrogens blue. (b) Structure of tubulin-RB3-TTL in complex with pironetin in which pironetin is bound to α2-tubulin. The protein subunits are shown in cartoon. The ligands are shown as spheres with atoms coloured as in a. (c) Close-up view of pironetin in the pocket of α-tubulin monomer. (d) Cross-section view of the surface of the binding pocket of pironetin. K352 previously reported to be modified is shown alongside other residues discussed in the text.
