5jld

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'''Unreleased structure'''
 
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The entry 5jld is ON HOLD until Paper Publication
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==Crystal Structure of Arginyl-tRNA Synthetase from Plasmodium falciparum (PfRRS)==
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<StructureSection load='5jld' size='340' side='right'caption='[[5jld]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5jld]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_falciparum_3D7 Plasmodium falciparum 3D7]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5JLD FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jld OCA], [https://pdbe.org/5jld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jld RCSB], [https://www.ebi.ac.uk/pdbsum/5jld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jld ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q8I5M2_PLAF7 Q8I5M2_PLAF7]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5jld" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Plasmodium falciparum 3D7]]
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[[Category: Jain V]]
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[[Category: Manickam Y]]
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[[Category: Sharma A]]

Current revision

Crystal Structure of Arginyl-tRNA Synthetase from Plasmodium falciparum (PfRRS)

PDB ID 5jld

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