Journal
CHEMISTRY & BIOLOGY
Volume 15, Issue 5, Pages 485-492Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2008.03.014
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Funding
- Austrian Science Fund (FWF) [Y 315] Funding Source: researchfish
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Peptide bond formation is a fundamental reaction in biology, catalyzed by the ribosomal peptidyl-transferase ribozyme. Although all active-site 23S ribosomal RNA nucleotides are universally conserved, atomic mutagenesis Suggests that these nucleo-bases do not carry functional groups directly involved in peptide bond formation. Instead, a single ribose 2-hydroxyl group at A2451 was identified to be of pivotal importance. Here, we altered the chemical characteristics by replacing its 2-hydroxyl with selected functional groups and demonstrate that hydrogen donor capability is essential for transpeptidation. We propose that the A2451-2'-hydroxyl directly hydrogen bonds to the P-site tRNA-A76 ribose. This promotes an effective A76 ribose C2'-endo conformation to support amide synthesis via a proton shuttle mechanism. Simultaneously, the direct interaction of A2451 with A76 renders the intramolecular transesterification of the pep-tide from the 3'- to 2'-oxygen unfeasible, thus promoting effective peptide bond synthesis.
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