Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism. (Articolo in rivista)

Type
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)
Pagina inizio
  • 20 (literal)
Pagina fine
  • 25 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 567 (literal)
Rivista
Note
  • 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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