2oe6
From Proteopedia
(New page: 200px<br /><applet load="2oe6" size="350" color="white" frame="true" align="right" spinBox="true" caption="2oe6, resolution 2.40Å" /> '''2.4A X-ray crystal s...) |
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==Overview== | ==Overview== | ||
| - | Aminoglycoside antibiotics bind specifically to the bacterial ribosomal | + | Aminoglycoside antibiotics bind specifically to the bacterial ribosomal decoding-site RNA and thereby interfere with fidelity but not efficiency of translation. Apramycin stands out among aminoglycosides for its mechanism of action which is based on blocking translocation and its ability to bind also to the eukaryotic decoding site despite differences in key residues required for apramycin recognition by the bacterial target. To elucidate molecular recognition of the eukaryotic decoding site by apramycin we have determined the crystal structure of an oligoribonucleotide containing the human sequence free and in complex with the antibiotic at 1.5 A resolution. The drug binds in the deep groove of the RNA which forms a continuously stacked helix comprising non-canonical C.A and G.A base pairs and a bulged-out adenine. The binding mode of apramycin at the human decoding-site RNA is distinct from aminoglycoside recognition of the bacterial target, suggesting a molecular basis for the actions of apramycin in eukaryotes and bacteria. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Apramycin recognition by the human ribosomal decoding site., Hermann T, Tereshko V, Skripkin E, Patel DJ, Blood Cells Mol Dis. 2007 | + | Apramycin recognition by the human ribosomal decoding site., Hermann T, Tereshko V, Skripkin E, Patel DJ, Blood Cells Mol Dis. 2007 May-Jun;38(3):193-8. Epub 2007 Jan 29. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17258916 17258916] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Hermann, T.]] | [[Category: Hermann, T.]] | ||
| - | [[Category: Patel, D | + | [[Category: Patel, D J.]] |
[[Category: Skripkin, E.]] | [[Category: Skripkin, E.]] | ||
[[Category: Tereshko, V.]] | [[Category: Tereshko, V.]] | ||
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[[Category: rna duplex]] | [[Category: rna duplex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:17:25 2008'' |
Revision as of 16:17, 21 February 2008
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2.4A X-ray crystal structure of unliganded RNA fragment GGGCGUCGCUAGUACC/CGGUACUAAAAGUCGCC containing the human ribosomal decoding A site: RNA construct with 5'-overhang
Overview
Aminoglycoside antibiotics bind specifically to the bacterial ribosomal decoding-site RNA and thereby interfere with fidelity but not efficiency of translation. Apramycin stands out among aminoglycosides for its mechanism of action which is based on blocking translocation and its ability to bind also to the eukaryotic decoding site despite differences in key residues required for apramycin recognition by the bacterial target. To elucidate molecular recognition of the eukaryotic decoding site by apramycin we have determined the crystal structure of an oligoribonucleotide containing the human sequence free and in complex with the antibiotic at 1.5 A resolution. The drug binds in the deep groove of the RNA which forms a continuously stacked helix comprising non-canonical C.A and G.A base pairs and a bulged-out adenine. The binding mode of apramycin at the human decoding-site RNA is distinct from aminoglycoside recognition of the bacterial target, suggesting a molecular basis for the actions of apramycin in eukaryotes and bacteria.
About this Structure
2OE6 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Apramycin recognition by the human ribosomal decoding site., Hermann T, Tereshko V, Skripkin E, Patel DJ, Blood Cells Mol Dis. 2007 May-Jun;38(3):193-8. Epub 2007 Jan 29. PMID:17258916
Page seeded by OCA on Thu Feb 21 18:17:25 2008
