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. 2021 Feb 8;40(6):e106449. doi: 10.15252/embj.2020106449

Figure EV5. The hydrophobic pocket of the eEF3 CD.

Figure EV5

  • A, B
    (A) Overview of the POST‐2 eEF3‐80S molecular model (B) highlighting the position of eEF3‐CD (green) relative to L1 protein (yellow) and ES30L (orange).
  • C, D
    (C) Same as (B) but for POST‐1, and (D) comparison of (B) and (C) depicting the magnitude of the L1‐stalk movement from the POST‐2 state (L1‐stalk′int′) to the POST‐1 state (L1‐stalk′in′). L1‐POST1 (light gray), ES30L‐POST1 (dark gray).
  • E, F
    (E) eEF3‐80S molecular model highlighting eEF3 (pale green) and the L1 protein (yellow) and its (F) zoom showing the magnitude of the distance between the eEF3‐CD hydrophobic pocket (based on the alignment with HP1 shown in (I)) and the K46 of the L1‐dI. K46* labels the lysine, which is getting methylated by the Seven‐β‐strand methyltransferase (Webb et al, 2011).
  • G, H
    (G) The eEF3‐CD hydrophobic pocket based on the alignment with (H) the D. melanogaster HP1‐CD.
  • I
    Overlay of the eEF3 and HP1 CD based on their sequence.