4twa: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4twa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TWA FirstGlance]. <br> | <table><tr><td colspan='2'>[[4twa]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TWA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TWA FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Proline--tRNA_ligase Proline--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.15 6.1.1.15] </span></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4twa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4twa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4twa RCSB], [http://www.ebi.ac.uk/pdbsum/4twa 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=4twa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4twa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4twa RCSB], [http://www.ebi.ac.uk/pdbsum/4twa PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Proline--tRNA ligase]] | [[Category: Proline--tRNA ligase]] | ||
[[Category: Jain, V | [[Category: Jain, V]] | ||
[[Category: Sharma, A | [[Category: Sharma, A]] | ||
[[Category: Yogavel, M | [[Category: Yogavel, M]] | ||
[[Category: Halofuginone]] | [[Category: Halofuginone]] | ||
[[Category: Inhibitor]] | [[Category: Inhibitor]] | ||
Revision as of 10:25, 3 December 2014
Crystal Structure of Prolyl-tRNA Synthetase (PRS) from Plasmodium falciparumCrystal Structure of Prolyl-tRNA Synthetase (PRS) from Plasmodium falciparum
Structural highlights
Publication Abstract from PubMedAminoacyl-tRNA synthetases (aaRSs) drive protein translation in cells and hence these are essential enzymes across life. Inhibition of these enzymes can halt growth of an organism by stalling protein translation. Therefore, small molecule targeting of aaRS active sites is an attractive avenue from the perspective of developing anti-infectives. Febrifugine and its derivatives like halofuginone (HF) are known to inhibit prolyl-tRNA synthetase of malaria parasite Plasmodium falciparum. Here, we present functional and crystallographic data on P. falciparum prolyl-tRNA synthetase (PfPRS). Using immunofluorescence data, we show that PfPRS is exclusively resident in the parasite cytoplasm within asexual blood stage parasites. The inhibitor HF interacts strongly with PfPRS in a non-competitive binding mode in presence or absence of ATP analog. Intriguingly, the two monomers that constitute dimeric PfPRS display significantly different conformations in their active site regions. The structural analyses presented here provide a framework for development of febrifugine derivatives that can seed development of new anti-malarials. Structural and functional analysis of the anti-malarial drug target prolyl-tRNA synthetase.,Jain V, Kikuchi H, Oshima Y, Sharma A, Yogavel M J Struct Funct Genomics. 2014 Jul 22. PMID:25047712[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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