1oln
From Proteopedia
(New page: 200px<br /><applet load="1oln" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oln" /> '''MODEL FOR THIOSTREPTON ANTIBIOTIC BINDING TO...) |
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'''MODEL FOR THIOSTREPTON ANTIBIOTIC BINDING TO L11 SUBSTRATE FROM 50S RIBOSOMAL RNA'''<br /> | '''MODEL FOR THIOSTREPTON ANTIBIOTIC BINDING TO L11 SUBSTRATE FROM 50S RIBOSOMAL RNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Thiostrepton and micrococcin inhibit protein synthesis by binding to the | + | 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== | ==About this Structure== | ||
| - | 1OLN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with THR, PYT, TZO, TZB, TZO, QUA and XBB as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1OLN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima] with <scene name='pdbligand=THR:'>THR</scene>, <scene name='pdbligand=PYT:'>PYT</scene>, <scene name='pdbligand=TZO:'>TZO</scene>, <scene name='pdbligand=TZB:'>TZB</scene>, <scene name='pdbligand=TZO:'>TZO</scene>, <scene name='pdbligand=QUA:'>QUA</scene> and <scene name='pdbligand=XBB:'>XBB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OLN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lentzen, G.]] | [[Category: Lentzen, G.]] | ||
[[Category: Matassova, N.]] | [[Category: Matassova, N.]] | ||
| - | [[Category: Murchie, A | + | [[Category: Murchie, A I.H.]] |
[[Category: PYT]] | [[Category: PYT]] | ||
[[Category: QUA]] | [[Category: QUA]] | ||
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[[Category: translation inhibition]] | [[Category: translation inhibition]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:03 2008'' |
Revision as of 12:19, 21 February 2008
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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 , , , , , and 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 Thu Feb 21 14:19:03 2008
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
