3bnp: Difference between revisions
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<StructureSection load='3bnp' size='340' side='right'caption='[[3bnp]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='3bnp' size='340' side='right'caption='[[3bnp]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3bnp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BNP OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[3bnp]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BNP FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bnl|3bnl]], [[3bnn|3bnn]], [[3bno|3bno]], [[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;'>[[3bnl|3bnl]], [[3bnn|3bnn]], [[3bno|3bno]], [[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=3bnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bnp OCA], [https://pdbe.org/3bnp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bnp RCSB], [https://www.ebi.ac.uk/pdbsum/3bnp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bnp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 09:49, 12 May 2022
Crystal Structure of the Homo sapiens Mitochondrial Ribosomal Decoding Site (A1555G Mutant)Crystal Structure of the Homo sapiens Mitochondrial Ribosomal Decoding Site (A1555G Mutant)
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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