3ugt: Difference between revisions
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==Crystal structure of the yeast mitochondrial threonyl-tRNA synthetase - orthorhombic crystal form== | ==Crystal structure of the yeast mitochondrial threonyl-tRNA synthetase - orthorhombic crystal form== | ||
<StructureSection load='3ugt' size='340' side='right' caption='[[3ugt]], [[Resolution|resolution]] 3.60Å' scene=''> | <StructureSection load='3ugt' size='340' side='right' caption='[[3ugt]], [[Resolution|resolution]] 3.60Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MST1, YKL194C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MST1, YKL194C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] </span></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=3ugt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ugt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ugt RCSB], [http://www.ebi.ac.uk/pdbsum/3ugt PDBsum]</span></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=3ugt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ugt OCA], [http://pdbe.org/3ugt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ugt RCSB], [http://www.ebi.ac.uk/pdbsum/3ugt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ugt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 3ugt" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 22:46, 11 August 2016
Crystal structure of the yeast mitochondrial threonyl-tRNA synthetase - orthorhombic crystal formCrystal structure of the yeast mitochondrial threonyl-tRNA synthetase - orthorhombic crystal form
Structural highlights
Publication Abstract from PubMedAminoacyl-tRNA synthetases (aaRSs) ensure faithful translation of mRNA into protein by coupling an amino acid to a set of tRNAs with conserved anticodon sequences. Here, we show that in mitochondria of Saccharomyces cerevisiae, a single aaRS (MST1) recognizes and aminoacylates two natural tRNAs that contain anticodon loops of different size and sequence. Besides a regular with a threonine (Thr) anticodon, MST1 also recognizes an unusual , which contains an enlarged anticodon loop and an anticodon triplet that reassigns the CUN codons from leucine to threonine. Our data show that MST1 recognizes the anticodon loop in both tRNAs, but employs distinct recognition mechanisms. The size but not the sequence of the anticodon loop is critical for recognition, whereas the anticodon sequence is essential for aminoacylation of . The crystal structure of MST1 reveals that, while lacking the N-terminal editing domain, the enzyme closely resembles the bacterial threonyl-tRNA synthetase (ThrRS). A detailed structural comparison with Escherichia coli ThrRS, which is unable to aminoacylate , reveals differences in the anticodon-binding domain that probably allow recognition of the distinct anticodon loops. Finally, our mutational and modeling analyses identify the structural elements in MST1 (e.g., helix alpha11) that define tRNA selectivity. Thus, MTS1 exemplifies that a single aaRS can recognize completely divergent anticodon loops of natural isoacceptor tRNAs and that in doing so it facilitates the reassignment of the genetic code in yeast mitochondria. Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment.,Ling J, Peterson KM, Simonovic I, Cho C, Soll D, Simonovic M Proc Natl Acad Sci U S A. 2012 Feb 17. PMID:22343532[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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