Fig. 1: Ribosomal proteins at the exit tunnel and their structural modification by CRISPR-Cas9 gene editing.
From: Modulating co-translational protein folding by rational design and ribosome engineering
a Structure of the 70S E. coli ribosome highlighting the exit tunnel (boxed). (inset) A magnified view of the loops from ribosomal proteins uL4, uL22, uL23 and uL24 that protrude into the tunnel and make contacts with FLN5 (grey) and α-synuclein (dark grey) NCs. b Circos plots87, showing the interactions formed between the NCs, FLN5 (left) and α-synuclein (right), and ribosomal proteins in the exit tunnel as observed in all-atom molecular dynamics simulations restrained with chemical shifts and residual dipolar couplings8 from NMR spectroscopy. The greyscale lines connecting NCs and the ribosomal proteins represent the extent (% of total frames) of inter-molecular interactions (see ‘Methods’). The loops of uL4, uL22, uL23 and uL24 that interact with both FLN5 and α-synuclein NCs are circled. c Structures of uL22, uL23 and uL24 proteins from E. coli (PDB:3JBU) superimposed with models of truncated (ΔL, blue) and inserted (+L, grey) tunnel loops, and sequences below. d CRISPR-Cas9 ribosomal mutants that were generated and used in this study. Black rectangles show the loop regions that were modified.
