Summary information and primary citation
- PDB-id
-
1njn;
DSSR-derived features in text and
JSON formats
- Class
- ribosome
- Method
- X-ray (3.7 Å)
- Summary
- The crystal structure of the 50s large ribosomal
subunit from deinococcus radiodurans complexed with the
antibiotic sparsomycin
- Reference
-
Bashan A, Agmon I, Zarivatch R, Schluenzen F, Harms JM,
Berisio R, Bartels H, Franceschi F, Auerbach T, Hansen
HA, Kossoy E, Kessler M, Yonath A (2003): "Structural
basis of the ribosomal machinery for Peptide bond
formation, translocation, and nascent chain
progression." Mol.Cell, 11,
91-102. doi: 10.1016/S1097-2765(03)00009-1.
- 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.
