Video 1. Conformational rearrangements of TbAdoMetDC upon dimerization with prozyme.
The movie shows the changes within TbAdoMetDC from its confirmation as a TbAdoMetDCΔ26 monomer to the CGP-bound TbAdoMetDC/prozyme heterodimer. TbAdoMetDC is colored by chain (β in pink, α in beige, prozyme in yellow). The ribbon representation is based on the monomer secondary structure assignment. Key residues are shown: F28 (pink sticks) interacts with Y243 (beige sticks) in the monomer and forms the CGP (purple sticks) binding site in the heterodimer; D169 (beige spheres) interacts with H172 (beige spheres) in the monomer and moves 14 Å in the heterodimer to form new interactions with Y152', K156', H163' (yellow sticks); G30-P31 (pink spheres) forms cis-peptidyl bond in the monomer that trans-isomerizes in the heterodimer; W137 (orange spheres) is part of the β6-h8 connector (orange) that is partially disordered and blocks the h1 binding pocket in the monomer while repositioning and becoming structured in the heterodimer; F163 and F165 (cyan spheres) and F174, Y176 (green spheres) are residues on β7 and β8 strands, respectively, that flip from one surface of the β-strands in the monomer to the opposite surface in a heterodimer; pyruvoyl group (beige spheres) is only shown for the heterodimer. The morph and the movie were generated with PyMOL.