Summary information and primary citation
- PDB-id
-
4ji1;
DSSR-derived features in text and
JSON formats
- Class
- ribosome-antibiotic
- Method
- X-ray (3.144 Å)
- Summary
- Crystal structure of 30s ribosomal subunit from thermus
thermophilus
- Reference
-
Demirci H, Wang L, Murphy FV, Murphy EL, Carr JF,
Blanchard SC, Jogl G, Dahlberg AE, Gregory ST (2013):
"The
central role of protein S12 in organizing the structure
of the decoding site of the ribosome." Rna,
19, 1791-1801. doi: 10.1261/rna.040030.113.
- Abstract
- The ribosome decodes mRNA by monitoring the geometry of
codon-anticodon base-pairing using a set of universally
conserved 16S rRNA nucleotides within the conformationally
dynamic decoding site. By applying single-molecule FRET and
X-ray crystallography, we have determined that
conditional-lethal, streptomycin-dependence mutations in
ribosomal protein S12 interfere with tRNA selection by
allowing conformational distortions of the decoding site
that impair GTPase activation of EF-Tu during the tRNA
selection process. Distortions in the decoding site are
reversed by streptomycin or by a second-site suppressor
mutation in 16S rRNA. These observations encourage a
refinement of the current model for decoding, wherein
ribosomal protein S12 and the decoding site collaborate to
optimize codon recognition and substrate discrimination
during the early stages of the tRNA selection process.
