Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression(595 views) Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HAS, Kossoy E, Kessler M, Yonath A
Keywords: Peptidyltransferase, Puromycin, Ribosome Rna, Transfer Rna, Article, Chemical Bond, Chemical Interaction, Conformational Transition, Crystal Structure, Deinococcus Radiodurans, Nonhuman, Protein Conformation, Ribosome Subunit, Rna Structure, Rna Transport, Bacterial Proteins, Catalytic Domain, Crystallography, X-Ray, Models, Molecular, Molecular Structure, Nucleic Acid Conformation, Protein Biosynthesis, Protein Synthesis Inhibitors, Ribosomal Proteins, Amino Acyl, Sparsomycin,
Affiliations: *** IBB - CNR ***
Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel
Max-Planck-Res. U. for Ribosomal S., Notkestrasse 85, 22603 Hamburg, Germany
FB Biologie, Chemie, Pharmazie, Frei University Berlin, Takustrasse 3, 14195 Berlin, Germany
Inst. of Biostructures and Bioimages, CNR, 80138 Napoli, Italy
References: Not available.
Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression
Crystal structures of tRNA mimics complexed with the large ribosomal subunit of Deinococcus radiodurans indicate that remote interactions determine the precise orientation of tRNA in the peptidyl-transferase center (PTC). The PTC tolerates various orientations of puromycin derivatives and its flexibility allows the conformational rearrangements required for peptide-bond formation. Sparsomycin binds to A2602 and alters the PTC conformation. H69, the intersubunit-bridge connecting the PTC and decoding site, may also participate in tRNA placement and translocation. A spiral rotation of the 3′ end of the A-site tRNA around a 2-fold axis of symmetry identified within the PTC suggests a unified ribosomal machinery for peptide-bond formation, A-to-P-site translocation, and entrance of nascent proteins into the exit tunnel. Similar 2-fold related regions, detected in all known structures of large ribosomal subunits, indicate the universality of this mechanism.
Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression