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5jld
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of Arginyl-tRNA Synthetase from Plasmodium falciparum (PfRRS)== | |
| + | <StructureSection load='5jld' size='340' side='right' caption='[[5jld]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jld]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JLD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JLD FirstGlance]. <br> | ||
| + | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arginine--tRNA_ligase Arginine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.19 6.1.1.19] </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=5jld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jld OCA], [http://pdbe.org/5jld PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jld RCSB], [http://www.ebi.ac.uk/pdbsum/5jld PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jld ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Excess cellular heme is toxic, and malaria parasites regulate its levels during hemoglobin digestion. Aminoacyl-tRNA synthetases are ubiquitous enzymes, and of these, arginyl-tRNA synthetase (RRS) is unique as its enzymatic product of charged tRNA is required for protein synthesis and degradation. We show that Plasmodium falciparum arginyl-tRNA synthetase (PfRRS) is an active, cytosolic, and monomeric enzyme. Its high-resolution crystal structure highlights critical structural differences with the human enzyme. We further show that hemin binds to and inhibits the aminoacylation activity of PfRRS. Hemin induces a dimeric form of PfRRS that is thus rendered enzymatically dead as it is unable to recognize its cognate tRNAarg. Excessive hemin in chloroquine-treated malaria parasites results in significantly reduced charged tRNAarg levels, thus suggesting deceleration of protein synthesis. These data together suggest that the inhibition of Plasmodium falciparum arginyl-tRNA synthetase can now be synergized with existing antimalarials for more potent drug cocktails against malaria parasites. | ||
| - | + | Dimerization of Arginyl-tRNA Synthetase by Free Heme Drives Its Inactivation in Plasmodium falciparum.,Jain V, Yogavel M, Sharma A Structure. 2016 Sep 6;24(9):1476-1487. doi: 10.1016/j.str.2016.06.018. Epub 2016 , Aug 5. PMID:27502052<ref>PMID:27502052</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5jld" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arginine--tRNA ligase]] | ||
| + | [[Category: Jain, V]] | ||
| + | [[Category: Manickam, Y]] | ||
| + | [[Category: Sharma, A]] | ||
| + | [[Category: Arginyl-trna synthetase]] | ||
| + | [[Category: Ligase]] | ||
| + | [[Category: Malaria]] | ||
| + | [[Category: Translation]] | ||
Revision as of 06:52, 10 September 2016
Crystal Structure of Arginyl-tRNA Synthetase from Plasmodium falciparum (PfRRS)
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