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.
| Predicate | Object |
|---|---|
| rdf:type | |
| rdfs:comment |
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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| skos:exactMatch | |
| uniprot:name |
Mol. Cell
|
| uniprot:author |
Agmon I.,
Auerbach T.,
Bartels H.,
Bashan A.,
Berisio R.,
Franceschi F.,
Hansen H.A.,
Harms J.,
Kessler M.,
Kossoy E.,
Schluenzen F.,
Yonath A.,
Zarivach R.
|
| uniprot:date |
2003
|
| uniprot:pages |
91-102
|
| uniprot:title |
Structural basis of the ribosomal machinery for peptide bond formation, translocation, and nascent chain progression.
|
| uniprot:volume |
11
|
| dc-term:identifier |
doi:10.1016/S1097-2765(03)00009-1
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