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. 2020 Dec 8;40(1):e105179. doi: 10.15252/embj.2020105179

Figure EV5. Model fitting and sequence alignment of the eIF3c‐NTD.

Figure EV5

  1. Overview of the TC‐containing human 43S PIC as shown in Fig 6 and scheme indicating the parts of eIF3c modeled. Black box indicates section of eIF3c highlighted in (B).
  2. Zoomed views highlighting fits of the eIF3c‐NTD 4‐helix bundle into the refined density (gray transparent mesh). The N‐ and C‐terminal residues are marked.
  3. MSA of the conserved N‐terminal region of eIF3c in mammals (Ser39‐Lys213 in H.s.), aligned with segments of the NTD from S.c.. Coloring according to default Clustal X color scheme (blue: hydrophobic, magenta: negative charge, red: positive charge, green: polar, orange: glycine, yellow: proline, pink: cysteine, cyan: aromatic). The 4‐helix bundle shows 31.1/67.2% sequence identity/similarity, and the eIF1‐interacting stretch present in the N‐terminus of S.c. eIF3c (Gln42‐Lys92) shows 32.0/56.0% sequence identity/similarity with a mammalia‐specific insert C‐terminal of the conserved 4‐helix bundle.
  4. eIF3c‐NTD in the human 43S PIC fitted into the cryo‐EM map and zoomed view showing the fit of the eIF1‐interacting stretch of eIF3c into the cryo‐EM map.