4j75: Difference between revisions
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==Crystal Structure of a parasite tRNA synthetase, product-bound== | ==Crystal Structure of a parasite tRNA synthetase, product-bound== | ||
<StructureSection load='4j75' size='340' side='right' caption='[[4j75]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4j75' size='340' side='right'caption='[[4j75]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4j75]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4j75]] is a 2 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=4J75 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J75 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TYM:TRYPTOPHANYL-5AMP'>TYM</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TYM:TRYPTOPHANYL-5AMP'>TYM</scene></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=4j75 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j75 OCA], [https://pdbe.org/4j75 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j75 RCSB], [https://www.ebi.ac.uk/pdbsum/4j75 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j75 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8IDW3_PLAF7 Q8IDW3_PLAF7] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4j75" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4j75" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Plasmodium falciparum 3D7]] | ||
[[Category: Hol | [[Category: Hol WGJ]] | ||
[[Category: Kim | [[Category: Kim JE]] | ||
[[Category: Koh | [[Category: Koh CY]] | ||
[[Category: Verlinde | [[Category: Verlinde CLMJ]] | ||
Revision as of 13:55, 24 November 2022
Crystal Structure of a parasite tRNA synthetase, product-boundCrystal Structure of a parasite tRNA synthetase, product-bound
Structural highlights
FunctionPublication Abstract from PubMedMalaria, most commonly caused by the parasite Plasmodium falciparum, is a devastating disease that remains a large global health burden. Lack of vaccines and drug resistance necessitate the continual development of new drugs and exploration of new drug targets. Due to their essential role in protein synthesis, aminoacyl-tRNA synthetases are potential anti-malaria drug targets. Here we report the crystal structures of P. falciparum cytosolic tryptophanyl-tRNA synthetase (Pf-cTrpRS) in its ligand-free state and tryptophanyl-adenylate (WAMP)-bound state at 2.34A and 2.40A resolutions, respectively. Large conformational changes are observed when the ligand-free protein is bound to WAMP. Multiple residues, completely surrounding the active site pocket, collapse onto WAMP. Comparison of the structures to those of human cytosolic TrpRS (Hs-cTrpRS) provides information about the possibility of targeting Pf-cTrpRS for inhibitor development. There is a high degree of similarity between Pf-cTrpRS and Hs-cTrpRS within the active site. However, the large motion that Pf-cTrpRS undergoes during transitions between different functional states avails an opportunity to arrive at compounds which selectively perturb the motion, and may provide a starting point for the development of new anti-malaria therapeutics. Crystal structures of Plasmodium falciparum cytosolic tryptophanyl-tRNA synthetase and its potential as a target for structure-guided drug design.,Koh CY, Kim JE, Napoli AJ, Verlinde CL, Fan E, Buckner FS, Van Voorhis WC, Hol WG Mol Biochem Parasitol. 2013 May 7;189(1-2):26-32. doi:, 10.1016/j.molbiopara.2013.04.007. PMID:23665145[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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