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| ==Crystal Structure of Blasticidin S Bound to Thermus Thermophilus 70S Ribosome. This file contains the 50S subunit and blasticidin S molecule from the first 70S ribosome.==
| | #REDIRECT [[4v9q]] This PDB entry is obsolete and replaced by 4v9q |
| <StructureSection load='4l6j' size='340' side='right' caption='[[4l6j]], [[Resolution|resolution]] 3.40Å' scene=''>
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| == Structural highlights ==
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| <table><tr><td colspan='2'>[[4l6j]] is a 30 chain structure with sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4L6J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4L6J FirstGlance]. <br>
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| </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BLS:BLASTICIDIN+S'>BLS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene><br>
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| <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4l6k|4l6k]], [[4l6l|4l6l]], [[4l6m|4l6m]]</td></tr>
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| <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4l6j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4l6j OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4l6j RCSB], [http://www.ebi.ac.uk/pdbsum/4l6j PDBsum]</span></td></tr>
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| <table>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| The antibiotic blasticidin S (BlaS) is a potent inhibitor of protein synthesis in bacteria and eukaryotes. We have determined a 3.4-A crystal structure of BlaS bound to a 70StRNA ribosome complex and performed biochemical and single-molecule FRET experiments to determine the mechanism of action of the antibiotic. We find that BlaS enhances tRNA binding to the P site of the large ribosomal subunit and slows down spontaneous intersubunit rotation in pretranslocation ribosomes. However, the antibiotic has negligible effect on elongation factor G catalyzed translocation of tRNA and mRNA. The crystal structure of the antibiotic-ribosome complex reveals that BlaS impedes protein synthesis through a unique mechanism by bending the 3' terminus of the P-site tRNA toward the A site of the large ribosomal subunit. Biochemical experiments demonstrate that stabilization of the deformed conformation of the P-site tRNA by BlaS strongly inhibits peptidyl-tRNA hydrolysis by release factors and, to a lesser extent, peptide bond formation.
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| Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome.,Svidritskiy E, Ling C, Ermolenko DN, Korostelev AA Proc Natl Acad Sci U S A. 2013 Jul 23;110(30):12283-8. doi:, 10.1073/pnas.1304922110. Epub 2013 Jul 3. PMID:23824292<ref>PMID:23824292</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| ==See Also==
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| *[[Ribosome 3D structures|Ribosome 3D structures]]
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| == References ==
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| <references/>
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| __TOC__
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| </StructureSection>
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| [[Category: Thermus thermophilus]]
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| [[Category: Ermolenko, D N.]]
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| [[Category: Korostelev, A A.]]
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| [[Category: Ling, C.]]
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| [[Category: Svidritskiy, E.]]
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| [[Category: Blasticidin s]]
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| [[Category: Peptidyl transfer]]
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| [[Category: Ribosomal crystal structure]]
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| [[Category: Ribosome]]
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| [[Category: Translation inhibitor]]
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| [[Category: Translation termination]]
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