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Ribosomal crystallography: a flexible nucleotide anchoring tRNA translocation, facilitates peptide-bond formation, chirality discrimination and antibiotics synergism Agmon I; Amit M; Auerbach T; Bashan A; Baram D; Bartels H; Berisio R; Greenberg I; Harms J; Hansen HA; Kessler M; Pyetan E; Schluenzen F; Sittner A; Yonath A; Zarivach RFEBS Lett 2004[Jun]; 567 (1): 20-6The 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.|Amino Acids/chemistry[MESH]|Anti-Bacterial Agents/chemistry[MESH]|Azithromycin/pharmacology[MESH]|Catalysis[MESH]|Crystallography, X-Ray/*methods[MESH]|Models, Molecular[MESH]|Peptides/chemistry[MESH]|Protein Isoforms[MESH]|Protein Structure, Tertiary[MESH]|Protein Transport[MESH]|RNA, Messenger/metabolism[MESH]|RNA, Transfer/chemistry/metabolism[MESH]|Ribosomes/*chemistry/*ultrastructure[MESH]|Substrate Specificity[MESH]|Virginiamycin/pharmacology[MESH] |
