Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression.

Article Details

Citation

Bashan A, Agmon I, Zarivach R, Schluenzen F, Harms J, Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen HA, Kossoy E, Kessler M, Yonath A

Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression.

Mol Cell. 2003 Jan;11(1):91-102.

PubMed ID
12535524 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
50S ribosomal protein L32P49228Details