1OLN

Model for thiostrepton antibiotic binding to L11 substrate from 50S ribosomal RNA

Summary for 1OLN

• Entry DOI: 10.2210/pdb1oln/pdb
• Related: 1D8T 1E9W 1EG0 1GIY 1JQM 1JQS 1JQT 1MMS 1PN7 1PN8 2C77 2JQ7 2ZJP 3CF5 487D
• Related PRD ID: PRD_000223
• Descriptor: 50S RIBOSOMAL PROTEIN L11, THIOSTREPTON, RNA (3 entities in total)
• Functional Keywords: ribosome-antibiotic complex, thiopeptide, antibacterial, thiazole, oxazole, ribosome, l11, translation inhibition, ribosome/antibiotic
• Biological source: THERMOTOGA MARITIMA; More
• Total number of polymer chains: 3
• Total formula weight: 35479.86

Authors

Lentzen, G.,Klinck, R.,Matassova, N.,Aboul-Ela, F.,Murchie, A.I.H. (deposition date: 2003-08-08, release date: 2003-09-11, Last modification date: 2025-04-09)

Primary citation

Lentzen, G.,Klinck, R.,Matassova, N.,Aboul-Ela, F.,Murchie, A.I.H.
Structural Basis for Contrasting Activities of Ribosome Binding Thiazole Antibiotics
Chem.Biol., 10:769-, 2003

PubMed 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.

PubMed: 12954336
DOI: 10.1016/S1074-5521(03)00173-X

Experimental method

SOLUTION NMR
THEORETICAL MODEL