Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism
| Autor: | Ilana Agmon, Joerg Harms, Maggie Kessler, David Baram, Assa Sittner, Ada Yonath, Maya Amit, Inbal Greenberg, Heike Bartels, Harly A. S. Hansen, Erez Pyetan, Tamar Auerbach, Rita Berisio, Frank Schluenzen, Anat Bashan, Raz Zarivach |
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| Rok vydání: | 2004 |
| Předmět: |
Models
Molecular Antibiotics synergism Stereochemistry Biophysics Azithromycin Biology Crystallography X-Ray Virginiamycin Biochemistry Ribosome Catalysis Substrate Specificity RNA Transfer Structural Biology Genetics Protein biosynthesis Protein Isoforms Peptide bond RNA Messenger Amino Acids Molecular Biology Dual binding Cell Biology Processivity Ribosomal RNA Synercid Peptide-bond formation Anti-Bacterial Agents Protein Structure Tertiary Protein Transport Transfer RNA Positional catalysis T arm Peptides Chirality (chemistry) Ribosomes |
| Zdroj: | FEBS letters 567 (2004): 20–25. doi:10.1016/j.febslet.2004.03.065 info:cnr-pdr/source/autori:Agmon, Ilana; Amit, Maya; Auerbach, Tamar; Bashan, Anat; Baram, David; Bartels, Heike; Berisio, Rita; Greenberg, Inbal; Harms, Joerg; Hansen, Harly A. S.; Kessler, Maggie; Pyetan, Erez; Schluenzen, Frank; Sittner, Assa; Yonath, Ada; Zarivach, Raz./titolo:Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism./doi:10.1016%2Fj.febslet.2004.03.065/rivista:FEBS letters (Print)/anno:2004/pagina_da:20/pagina_a:25/intervallo_pagine:20–25/volume:567 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/j.febslet.2004.03.065 |
| Popis: | The linkage between internal ribosomal symmetry and transfer RNA (tRNA) positioning confirmed positional catalysis of amino-acid polymerization. Peptide bonds are formed concurrently with tRNA-3′end rotatory motion, in conjunction with the overall messenger RNA (mRNA)/tRNA translocation. Accurate substrate alignment, mandatory for the processivity of protein biosynthesis, is governed by remote interactions. Inherent flexibility of a conserved nucleotide, anchoring the rotatory motion, facilitates chirality discrimination and antibiotics synergism. Potential tRNA interactions explain the universality of the tRNA CCA-end and P-site preference of initial tRNA. The interactions of protein L2 tail with the symmetry-related region periphery explain its conservation and its contributions to nascent chain elongation. |
| Databáze: | OpenAIRE |
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