Ribosome crystallography: catalysis and evolution of peptide-bond formation, nascent chain elongation and its co-translational folding
- 1 June 2005
- journal article
- review article
- Published by Portland Press Ltd. in Biochemical Society Transactions
- Vol. 33 (3) , 488-492
- https://doi.org/10.1042/bst0330488
Abstract
A ribosome is a ribozyme polymerizing amino acids, exploiting positional- and substrate-mediated chemical catalysis. We showed that peptide-bond formation is facilitated by the ribosomal architectural frame, provided by a sizable symmetry-related region in and around the peptidyl transferase centre, suggesting that the ribosomal active site was evolved by gene fusion. Mobility in tunnel components is exploited for elongation arrest as well as for trafficking nascent proteins into the folding space bordered by the bacterial chaperone, namely the trigger factor.Keywords
This publication has 32 references indexed in Scilit:
- From peptide‐bond formation to cotranslational folding: dynamic, regulatory and evolutionary aspectsFEBS Letters, 2004
- The Active Site of the Ribosome Is Composed of Two Layers of Conserved Nucleotides with Distinct Roles in Peptide Bond Formation and Peptide ReleaseCell, 2004
- Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide‐bond formation, chirality discrimination and antibiotics synergismFEBS Letters, 2004
- On peptide bond formation, translocation, nascent protein progression and the regulatory properties of ribosomesEuropean Journal of Biochemistry, 2003
- Molecular Chaperones in the Cytosol: from Nascent Chain to Folded ProteinScience, 2002
- Mechanism of Ribosomal Peptide Bond FormationScience, 2001
- The Structural Basis of Ribosome Activity in Peptide Bond SynthesisScience, 2000
- The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å ResolutionScience, 2000
- Substrate‐assisted catalysis: Molecular basis and biological significanceProtein Science, 2000
- Quantification of tertiary structural conservation despite primary sequence drift in the globin foldProtein Science, 1994