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| | ==Crystal structure of lysyl-tRNA synthetase LysRS from Burkholderia thailandensis bound to lysine== | | ==Crystal structure of lysyl-tRNA synthetase LysRS from Burkholderia thailandensis bound to lysine== |
| - | <StructureSection load='4ex5' size='340' side='right' caption='[[4ex5]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4ex5' size='340' side='right'caption='[[4ex5]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4ex5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EX5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EX5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4ex5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_thailandensis_E264 Burkholderia thailandensis E264]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EX5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EX5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] </span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LYS:LYSINE'>LYS</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=4ex5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ex5 OCA], [http://pdbe.org/4ex5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ex5 RCSB], [http://www.ebi.ac.uk/pdbsum/4ex5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ex5 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ex5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ex5 OCA], [https://pdbe.org/4ex5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ex5 RCSB], [https://www.ebi.ac.uk/pdbsum/4ex5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ex5 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/SYK_BURTA SYK_BURTA] |
| - | Aminoacyl-tRNA synthetases (aaRSs) charge tRNAs with their cognate amino acid, an essential precursor step to loading of charged tRNAs onto the ribosome and addition of the amino acid to the growing polypeptide chain during protein synthesis. Because of this important biological function, aminoacyl-tRNA synthetases have been the focus of anti-infective drug development efforts and two aaRS inhibitors have been approved as drugs. Several researchers in the scientific community requested aminoacyl-tRNA synthetases to be targeted in the Seattle Structural Genomics Center for Infectious Disease (SSGCID) structure determination pipeline. Here we investigate thirty-one aminoacyl-tRNA synthetases from infectious disease organisms by co-crystallization in the presence of their cognate amino acid, ATP, and/or inhibitors. Crystal structures were determined for a CysRS from Borrelia burgdorferi bound to AMP, GluRS from Borrelia burgdorferi and Burkholderia thailandensis bound to glutamic acid, a TrpRS from the eukaryotic pathogen Encephalitozoon cuniculi bound to tryptophan, a HisRS from Burkholderia thailandensis bound to histidine, and a LysRS from Burkholderia thailandensis bound to lysine. Thus, the presence of ligands may promote aaRS crystallization and structure determination. Comparison with homologous structures shows conformational flexibility that appears to be a recurring theme with this enzyme class.
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| - | Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms.,Moen SO, Edwards TE, Dranow DM, Clifton MC, Sankaran B, Van Voorhis WC, Sharma A, Manoil C, Staker BL, Myler PJ, Lorimer DD Sci Rep. 2017 Mar 16;7(1):223. doi: 10.1038/s41598-017-00367-6. PMID:28303005<ref>PMID:28303005</ref>
| + | ==See Also== |
| - | | + | *[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| - | </div>
| + | |
| - | <div class="pdbe-citations 4ex5" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lysine--tRNA ligase]] | + | [[Category: Burkholderia thailandensis E264]] |
| - | [[Category: Structural genomic]] | + | [[Category: Large Structures]] |
| - | [[Category: Aminoacyl-trna synthetase]]
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| - | [[Category: Atp-depenedent]]
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| - | [[Category: Class iib trna synthetase]]
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| - | [[Category: Lysine trna ligase]]
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| - | [[Category: National institute of allergy and infectious disease]]
| + | |
| - | [[Category: Niaid]]
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| - | [[Category: Protein synthesis]]
| + | |
| - | [[Category: Ssgcid]]
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| - | [[Category: Transferase]]
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| - | [[Category: Trnaly]]
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