An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA

T. Martin Schmeing, Kevin S. Huang, Scott A. Strobel and Thomas A. Steitz ()
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T. Martin Schmeing: Department of Molecular Biophysics and Biochemistry
Kevin S. Huang: Department of Molecular Biophysics and Biochemistry
Scott A. Strobel: Department of Molecular Biophysics and Biochemistry
Thomas A. Steitz: Department of Molecular Biophysics and Biochemistry

Nature, 2005, vol. 438, issue 7067, 520-524

Abstract: Don't go near the water Many kinds of enzymes need to protect their substrates from unwanted hydrolysis. Koshland proposed more than 40 years ago that these enzymes — he was looking specifically at hexokinase — adopt the catalytically competent conformation only when the appropriate substrates are bound and produce an ‘induced fit’ conformational change. Later work showed that it is indeed ‘induced fit’ that stops hexokinase from hydrolysing ATP when there is no glucose about. Structural studies of the large ribosomal subunit now show that a similar fit mechanism operates here too. This provides the answer to the long-standing question of how the nascent peptide in the P site of the ribosome avoids hydrolysis by peptidyl tRNA until the termination step of protein synthesis. This mechanism may well have been available to the ribozymes in an RNA world before proteins came on the scene.

Date: 2005
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DOI: 10.1038/nature04152

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