Visualization of elongation factor Tu on the Escherichia coli ribosome

Holger Stark, Marina V. Rodnina, Jutta Rinke-Appel, Richard Brimacombe, Wolfgang Wintermeyer and Marin van Heel ()
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Holger Stark: Imperial College of Science, Medicine and Technology
Marina V. Rodnina: Institut fr Molekularbiologie, Universitt Witten/Herdecke
Jutta Rinke-Appel: Max-Planck-Institut fr Molekulare Genetik
Richard Brimacombe: Max-Planck-Institut fr Molekulare Genetik
Wolfgang Wintermeyer: Institut fr Molekularbiologie, Universitt Witten/Herdecke
Marin van Heel: Imperial College of Science, Medicine and Technology

Nature, 1997, vol. 389, issue 6649, 403-406

Abstract: Abstract The delivery of a specific amino acid to the translating ribosome is fundamental to protein synthesis. The binding of aminoacyl-transfer RNA to the ribosome is catalysed by the elongation factor Tu (EF-Tu). The elongation factor, the aminoacyl-tRNA and GTP form a stable ‘ternary’ complex that binds to the ribosome. We have used electron cryomicroscopy and angular reconstitution1 to visualize directly the kirromycin-stalled ternary complex in the A site of the 70S ribosome of Escherichia coli. Electron cryomicroscopy had previously given detailed ribosomal structures at 25 and 23 Å (refs 2, 3) resolution, and was used to determine the position of tRNAs on the ribosome4,5. In particular, the structures5 of pre-translocational (tRNAs in A and P sites) and post-translocational ribosomes (P and E sites occupied) were both visualized at a resolution of ∼20 Å. Our three-dimensional reconstruction at 18 Å resolution shows the ternary complex spanning the inter-subunit space with the acceptor domain of the tRNA reaching into the decoding centre. Domain 1 (the G domain) of the EF-Tu is bound both to the L7/L12 stalk and to the 50S body underneath the stalk, whereas domain 2 is oriented towards the S12 region on the 30S subunit.

Date: 1997
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DOI: 10.1038/38770

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