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

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

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.

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Department of Structural Biology, Weizmann Institute, 76100 Rehovot, Israel.

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.

PMID:: 12535524; [PubMed - indexed for MEDLINE]

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Structures reported by this article

The Crystal Structure Of The 50s Large Ribosomal Subunit From Deinococcus Radiodurans Complexed With A Short Substrate Analog Accpuromycin (Accp)

PDB: 1NJO

Source: Deinococcus radiodurans, synthetic construct

Method: X-Ray Diffraction

Resolution: 3.7 Å

See all 4 structures...

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