3bnl: Difference between revisions
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<StructureSection load='3bnl' size='340' side='right'caption='[[3bnl]], [[Resolution|resolution]] 2.60Å' scene=''> | <StructureSection load='3bnl' size='340' side='right'caption='[[3bnl]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bnl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BNL OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3bnl]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BNL FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NCO:COBALT+HEXAMMINE(III)'>NCO</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bnn|3bnn]], [[3bno|3bno]], [[3bnp|3bnp]], [[3bnq|3bnq]], [[3bnr|3bnr]], [[3bns|3bns]], [[3bnt|3bnt]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bnn|3bnn]], [[3bno|3bno]], [[3bnp|3bnp]], [[3bnq|3bnq]], [[3bnr|3bnr]], [[3bns|3bns]], [[3bnt|3bnt]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bnl OCA], [https://pdbe.org/3bnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bnl RCSB], [https://www.ebi.ac.uk/pdbsum/3bnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bnl ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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</div> | </div> | ||
<div class="pdbe-citations 3bnl" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3bnl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:49, 12 May 2022
Crystal structure of the bacterial ribosomal decoding A site in the presence of [Co(NH3)6]Cl3Crystal structure of the bacterial ribosomal decoding A site in the presence of [Co(NH3)6]Cl3
Structural highlights
Publication Abstract from PubMedThe A site of the small ribosomal subunit participates in the fidelity of decoding by switching between two states, a resting 'off' state and an active decoding 'on' state. Eight crystal structures of RNA duplexes containing two minimal decoding A sites of the Homo sapiens mitochondrial wild-type, the A1555G mutant or bacteria have been solved. The resting 'off' state of the mitochondrial wild-type A site is surprisingly different from that of the bacterial A site. The mitochondrial A1555G mutant has two types of the 'off' states; one is similar to the mitochondrial wild-type 'off' state and the other is similar to the bacterial 'off' state. Our present results indicate that the dynamics of the A site in bacteria and mitochondria are different, a property probably related to the small number of tRNAs used for decoding in mitochondria. Based on these structures, we propose a hypothesis for the molecular mechanism of non-syndromic hearing loss due to the mitochondrial A1555G mutation. The bacterial and mitochondrial ribosomal A-site molecular switches possess different conformational substates.,Kondo J, Westhof E Nucleic Acids Res. 2008 May;36(8):2654-66. Epub 2008 Mar 16. PMID:18346970[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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