How ribosomes make peptide bonds

2007 | review. A publication with affiliation to the University of Göttingen.

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​How ribosomes make peptide bonds​
Rodnina, M. ; Beringer, M.& Wintermeyer, W. ​ (2007)
Trends in Biochemical Sciences, 32​(1) pp. 20​-26​.​
Elsevier Science London. DOI: https://doi.org/10.1016/j.tibs.2006.11.007 

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Authors
Rodnina, Marina ; Beringer, Malte; Wintermeyer, Wolfgang 
Abstract
Ribosomes are molecular machines that synthesize proteins in the cell. Recent biochemical analyses and high-resolution crystal structures of the bacterial ribosome have shown that the active site for the formation of peptide bonds - the peptidyl-transferase center - is composed solely of rRNA. Thus, the ribosome is the largest known RNA catalyst and the only natural ribozyme that has a synthetic activity. The ribosome employs entropic catalysis to accelerate peptide-bond formation by positioning substrates, reorganizing water in the active site and providing an electrostatic network that stabilizes reaction intermediates. Proton transfer during the reaction seems to be promoted by a concerted shuttle mechanism that involves ribose hydroxyl groups on the tRNA substrate.
Issue Date
2007
Publisher
Elsevier Science London
Journal
Trends in Biochemical Sciences 
ISSN
0968-0004

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