Summary information and primary citation
- PDB-id
-
1oln;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ribosome-antibiotic
- Method
- multiple methods: solution nmr, theoretical model
- Summary
- Model for thiostrepton antibiotic binding to l11
substrate from 50s ribosomal RNA
- Reference
-
Lentzen G, Klinck R, Matassova N, Aboul-Ela F, Murchie
AIH (2003): "Structural
Basis for Contrasting Activities of Ribosome Binding
Thiazole Antibiotics." Chem.Biol.,
10, 769. doi: 10.1016/S1074-5521(03)00173-X.
- Abstract
- Thiostrepton and micrococcin inhibit protein synthesis
by binding to the L11 binding domain (L11BD) of 23S
ribosomal RNA. The two compounds are structurally related,
yet they produce different effects on ribosomal RNA in
footprinting experiments and on elongation factor-G
(EF-G)-dependent GTP hydrolysis. Using NMR and an assay
based on A1067 methylation by thiostrepton-resistance
methyltransferase, we show that the related thiazoles,
nosiheptide and siomycin, also bind to this region. The
effect of all four antibiotics on EF-G-dependent GTP
hydrolysis and EF-G-GDP-ribosome complex formation was
studied. Our NMR and biochemical data demonstrate that
thiostrepton, nosiheptide, and siomycin share a common
profile, which differs from that of micrococcin. We have
generated a three-dimensional (3D) model for the
interaction of thiostrepton with L11BD RNA. The model
rationalizes the differences between micrococcin and the
thiostrepton-like antibiotics interacting with L11BD.
