Journal
MOLECULAR CELL
Volume 11, Issue 1, Pages 91-102Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(03)00009-1
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Funding
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM034360] Funding Source: NIH RePORTER
- NIGMS NIH HHS [GM34360] Funding Source: Medline
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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.
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