2m4q
From Proteopedia
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| - | + | ==NMR structure of E. coli ribosomela decoding site with apramycin== | |
| - | + | <StructureSection load='2m4q' size='340' side='right' caption='[[2m4q]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2m4q]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2M4Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2M4Q FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AM2:APRAMYCIN'>AM2</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2m4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m4q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2m4q RCSB], [http://www.ebi.ac.uk/pdbsum/2m4q PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Inferring antibiotic mechanisms on translation through static structures has been challenging, as biological systems are highly dynamic. Dynamic single-molecule methods are also limited to few simultaneously measurable parameters. We have circumvented these limitations with a multifaceted approach to investigate three structurally distinct aminoglycosides that bind to the aminoacyl-transfer RNA site (A site) in the prokaryotic 30S ribosomal subunit: apramycin, paromomycin, and gentamicin. Using several single-molecule fluorescence measurements combined with structural and biochemical techniques, we observed distinct changes to translational dynamics for each aminoglycoside. While all three drugs effectively inhibit translation elongation, their actions are structurally and mechanistically distinct. Apramycin does not displace A1492 and A1493 at the decoding center, as demonstrated by a solution nuclear magnetic resonance structure, causing only limited miscoding; instead, it primarily blocks translocation. Paromomycin and gentamicin, which displace A1492 and A1493, cause significant miscoding, block intersubunit rotation, and inhibit translocation. Our results show the power of combined dynamics, structural, and biochemical approaches to elucidate the complex mechanisms underlying translation and its inhibition. | ||
| - | + | The impact of aminoglycosides on the dynamics of translation elongation.,Tsai A, Uemura S, Johansson M, Puglisi EV, Marshall RA, Aitken CE, Korlach J, Ehrenberg M, Puglisi JD Cell Rep. 2013 Feb 21;3(2):497-508. doi: 10.1016/j.celrep.2013.01.027. Epub 2013 , Feb 14. PMID:23416053<ref>PMID:23416053</ref> | |
| - | + | ||
| - | [[Category: Marshall, R | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | [[Category: Puglisi, J D | + | </div> |
| - | [[Category: Tsai, A | + | == References == |
| - | [[Category: Viani, E | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Marshall, R]] | ||
| + | [[Category: Puglisi, J D]] | ||
| + | [[Category: Tsai, A]] | ||
| + | [[Category: Viani, E]] | ||
[[Category: Aminoglycoside]] | [[Category: Aminoglycoside]] | ||
[[Category: Antibiotic]] | [[Category: Antibiotic]] | ||
Revision as of 12:51, 18 December 2014
NMR structure of E. coli ribosomela decoding site with apramycin
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