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. 2007 Mar 26;104(14):5788–5793. doi: 10.1073/pnas.0606880104

Fig. 4.

Fig. 4.

Analysis of the 43S complex. (A) Orthogonal views of the platform/body region of the 20-Å 43S reconstruction (as in Fig. 3A) with the platform and body colored as in 2C and the MFC colored magenta, oriented such that the body is in the same orientation in each image as in Fig. 2C. Thumbnails show the 40S platform and body aligned by reference to the body of the 43S for each view. Thumbnails are 50% of the main image size. (B) Equivalent views to A in which the 43S density corresponding to the reordered small subunit is colored gray (using the head from 3B for the head and the 20-Å structure (A) for the body/platform) fitted with the atomic models for the head, platform, and body (13), colored blue, green, and red. The MFC density is shown as a mesh surface, colored magenta. Thumbnails of the MFC within the 43S (semitransparent surface) superimposed on the isolated MFC reconstruction (magenta mesh) are shown in each orientation. Asterisk, helix 18. Thumbnails are 75% of the main image size. (C) Schematic diagram of the conformational changes observed here in the 40S subunit (Left, inactive) on binding the eIFs that form the MFC (Center). The head is colored blue and the platform/body is yellow in each case, as in Figs. 2C and 3, with arrows indicating the domain movements after eIF binding that release the subunit head. (Center) The head displays movement along with the covalent link between it and the body. (Right) The small subunit has reverted to its usual structure within the elongating ribosome with the binding of the large 60S subunit. h, head; p, platform; b, body; mfc, multifactor complex.