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. Author manuscript; available in PMC: 2016 Sep 24.
Published in final edited form as: Nature. 2015 Sep 7;525(7570):491–495. doi: 10.1038/nature14891

Extended Data Fig. 10. Shape and ribosomal binding site of eIF3d, and eIF3b sequence.

Extended Data Fig. 10

a, Segmented cryo-EM reconstruction of the peripheral eIF3d subunit localized on the head of the 40S subunit, behind ribosomal protein RACK1, displayed at a high density threshold in order to show its most solid features, in four different orientations. b, eIF3d subunit in the context of the 43S preinitiation complex, seen from the back, showing the ribosomal proteins that contact it directly. This figure is complementary to Fig. 4c as it displays the same complex in a different orientation. This panel shows contacts between eIF3d subunit and ribosomal proteins eS28, uS7 and uS9. Contacts with RACK1 cannot be seen from this orientation. c, eIF3b sequence. The amino acid sequences of human eIF3b (GenBank NP_003742.2) and rabbit eIF3b (UniProt G1SZ03_RABIT) aligned using T_COFFEE (http://www.ebi.ac.uk/Tools/msa/tcoffee/) and annotated to show identity with tryptic and chymotryptic peptides derived from purified rabbit eIF3 and identified by nanoLC-MS/MS analysis. The complete sequence of rabbit eIF3b has not been determined, but clearly extends beyond the N-terminus of G1SZ03_RABIT, and we therefore used the numbering of residues in human eIF3b when referring in the text to elements of rabbit eIF3b.