1oln
From Proteopedia
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MODEL FOR THIOSTREPTON ANTIBIOTIC BINDING TO L11 SUBSTRATE FROM 50S RIBOSOMAL RNA
Overview
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.
About this Structure
1OLN is a Protein complex structure of sequences from Thermotoga maritima with THR, PYT, TZO, TZB, TZO, QUA and XBB as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for contrasting activities of ribosome binding thiazole antibiotics., Lentzen G, Klinck R, Matassova N, Aboul-ela F, Murchie AI, Chem Biol. 2003 Aug;10(8):769-78. PMID:12954336
Page seeded by OCA on Tue Nov 20 22:59:38 2007
Categories: Protein complex | Thermotoga maritima | Aboul-Ela, F. | Klinck, R. | Lentzen, G. | Matassova, N. | Murchie, A.I.H. | PYT | QUA | THR | TZB | TZO | XBB | 50s | Antibiotic | L11 | Ribosome | Rna | Thiazole | Thiostrepton | Translation inhibition
