http://www.cnr.it/ontology/cnr/individuo/prodotto/ID13446
Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism. (Articolo in rivista)
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- Label
- Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism. (Articolo in rivista) (literal)
- Anno
- 2004-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1016/j.febslet.2004.03.065 (literal)
- Alternative label
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. (2004)
Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism.
in FEBS letters (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#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. (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Agmon, Ilana; Amit, Maya; Auerbach, Tamar; Bashan, Anat; Baram, David; Greenberg, Inbal; Kessler, Maggie; Pyetan, Erez; Sittner, Assa : The Weizmann Institute, 76100 Rehovot, Israel
Bartels, Heike; Harms, Joerg; Hansen, Harly A. S.; Schluenzen, Frank; Yonath, Ada; Zarivach, Raz:
Max Planck Institute, Hamburg, Germany.
Berisio, Rita; IBB CNR (literal)
- Titolo
- Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism. (literal)
- Abstract
- The linkage between internal ribosomal symmetry and tRNA (tRNA) positioning confirmed positional catalysis of amino-acid polymn. Peptide bonds are formed concurrently with tRNA-3'end rotatory motion, in conjunction with the overall mRNA (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. (literal)
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