Literature DB >> 17499039

The ribosomal peptidyl transferase.

Malte Beringer1, Marina V Rodnina.   

Abstract

Peptide bond formation on the ribosome takes place in an active site composed of RNA. Recent progress of structural, biochemical, and computational approaches has provided a fairly detailed picture of the catalytic mechanism of the reaction. The ribosome accelerates peptide bond formation by lowering the activation entropy of the reaction due to positioning the two substrates, ordering water in the active site, and providing an electrostatic network that stabilizes the reaction intermediates. Proton transfer during the reaction appears to be promoted by a concerted proton shuttle mechanism that involves ribose hydroxyl groups on the tRNA substrate.

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Year:  2007        PMID: 17499039     DOI: 10.1016/j.molcel.2007.03.015

Source DB:  PubMed          Journal:  Mol Cell        ISSN: 1097-2765            Impact factor:   17.970


  52 in total

1.  pH-sensitivity of the ribosomal peptidyl transfer reaction dependent on the identity of the A-site aminoacyl-tRNA.

Authors:  Magnus Johansson; Ka-Weng Ieong; Stefan Trobro; Peter Strazewski; Johan Åqvist; Michael Y Pavlov; Måns Ehrenberg
Journal:  Proc Natl Acad Sci U S A       Date:  2010-12-17       Impact factor: 11.205

2.  Two distinct components of release factor function uncovered by nucleophile partitioning analysis.

Authors:  Jeffrey J Shaw; Rachel Green
Journal:  Mol Cell       Date:  2007-11-09       Impact factor: 17.970

Review 3.  Ribozyme catalysis revisited: is water involved?

Authors:  Nils G Walter
Journal:  Mol Cell       Date:  2007-12-28       Impact factor: 17.970

Review 4.  A gripping tale of ribosomal frameshifting: extragenic suppressors of frameshift mutations spotlight P-site realignment.

Authors:  John F Atkins; Glenn R Björk
Journal:  Microbiol Mol Biol Rev       Date:  2009-03       Impact factor: 11.056

5.  Transition state chirality and role of the vicinal hydroxyl in the ribosomal peptidyl transferase reaction.

Authors:  Kevin S Huang; Nicolas Carrasco; Emmanuel Pfund; Scott A Strobel
Journal:  Biochemistry       Date:  2008-08-02       Impact factor: 3.162

6.  RNA-assisted catalysis in a protein enzyme: The 2'-hydroxyl of tRNA(Thr) A76 promotes aminoacylation by threonyl-tRNA synthetase.

Authors:  Anand Minajigi; Christopher S Francklyn
Journal:  Proc Natl Acad Sci U S A       Date:  2008-11-07       Impact factor: 11.205

7.  Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.

Authors:  Kazuko Fujiwara; Nobuo Maita; Harumi Hosaka; Kazuko Okamura-Ikeda; Atsushi Nakagawa; Hisaaki Taniguchi
Journal:  J Biol Chem       Date:  2010-01-19       Impact factor: 5.157

Review 8.  A new view of protein synthesis: mapping the free energy landscape of the ribosome using single-molecule FRET.

Authors:  James B Munro; Andrea Vaiana; Kevin Y Sanbonmatsu; Scott C Blanchard
Journal:  Biopolymers       Date:  2008-07       Impact factor: 2.505

9.  Towards Accurate Prediction of Protonation Equilibrium of Nucleic Acids.

Authors:  Garrett B Goh; Jennifer L Knight; Charles L Brooks
Journal:  J Phys Chem Lett       Date:  2013-02-12       Impact factor: 6.475

10.  pH-dependent dynamics of complex RNA macromolecules.

Authors:  Garrett B Goh; Jennifer L Knight; Charles L Brooks
Journal:  J Chem Theory Comput       Date:  2013-01-03       Impact factor: 6.006

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