eEF2 (eukaryotic elongation factor 2) occupies an essential role in protein synthesis where it catalyses the translocation of the two tRNAs and the mRNA after peptidyl transfer on the 80 S ribosome. Recent crystal structures of eEF2 and the cryo-electron microscopy reconstruction of its 80 S complex now provide a substantial structural framework for dissecting the functional properties of this factor. The factor can be modified by either phosphorylation or ADP-ribosylation, which results in cessation of translation. We review the structural and functional properties of eEF2 with particular emphasis on the unique diphthamide residue, which is ADP-ribosylated by diphtheria toxin from Corynebacterium diphtheriae and exotoxin A from Pseudomonas aeruginosa.
Conference Article| January 20 2006
The life and death of translation elongation factor 2
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R. Jørgensen, A.R. Merrill, G.R. Andersen; The life and death of translation elongation factor 2. Biochem Soc Trans 1 February 2006; 34 (1): 1–6. doi: https://doi.org/10.1042/BST0340001
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