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Annu Rev Biochem. 2013;82:203-36. doi: 10.1146/annurev-biochem-113009-092313.

Structural basis of the translational elongation cycle.

Author information

1
MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom. voorhees@mrc-lmb.cam.ac.uk

Abstract

The sequential addition of amino acids to a growing polypeptide chain is carried out by the ribosome in a complicated multistep process called the elongation cycle. It involves accurate selection of each aminoacyl tRNA as dictated by the mRNA codon, catalysis of peptide bond formation, and movement of the tRNAs and mRNA through the ribosome. The process requires the GTPase factors elongation factor Tu (EF-Tu) and EF-G. Not surprisingly, large conformational changes in both the ribosome and its tRNA substrates occur throughout protein elongation. Major advances in our understanding of the elongation cycle have been made in the past few years as a result of high-resolution crystal structures that capture various states of the process, as well as biochemical and computational studies.

[Indexed for MEDLINE]

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