2oe5: Difference between revisions

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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oe5 OCA], [https://pdbe.org/2oe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oe5 RCSB], [https://www.ebi.ac.uk/pdbsum/2oe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oe5 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2oe5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2oe5 OCA], [https://pdbe.org/2oe5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2oe5 RCSB], [https://www.ebi.ac.uk/pdbsum/2oe5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2oe5 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:17258916</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2oe5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>

Latest revision as of 06:29, 3 April 2024

1.5 A X-ray crystal structure of Apramycin complex with RNA fragment GGCGUCGCUAGUACCG/GGUACUAAAAGUCGCCC containing the human ribosomal decoding A site: RNA construct with 3'-overhang

2oe5, resolution 1.51Å

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