6aa0
From Proteopedia
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<StructureSection load='6aa0' size='340' side='right'caption='[[6aa0]], [[Resolution|resolution]] 3.20Å' scene=''> | <StructureSection load='6aa0' size='340' side='right'caption='[[6aa0]], [[Resolution|resolution]] 3.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6aa0]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AA0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6aa0]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Toxgm Toxgm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AA0 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></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TGME49_219850 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=508771 TOXGM])</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 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 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=6aa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aa0 OCA], [http://pdbe.org/6aa0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aa0 RCSB], [http://www.ebi.ac.uk/pdbsum/6aa0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aa0 ProSAT]</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=6aa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aa0 OCA], [http://pdbe.org/6aa0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aa0 RCSB], [http://www.ebi.ac.uk/pdbsum/6aa0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aa0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Prolyl-tRNA synthetase (PRS) is a member of the aminoacyl-tRNA synthetase family that drives protein translation in cells. The apicomplexan PRSs are validated targets of febrifugine (FF) and its halogenated derivative halofuginone (HF). PRSs are of great interest for drug development against Plasmodium falciparum and Toxoplasma gondii. In this study, structures of apo and FF-bound T. gondii (TgPRS) are revealed and the dynamic nature of the conformational changes that occur upon FF binding is unraveled. In addition, this study highlights significant conformational plasticity within two different crystal structures of apo PRSs but not within drug-bound PRSs. The apo PRSs exist in multi-conformational states and manifest pseudo-dimeric structures. In contrast, when FF is bound the PRS dimer adopts a highly symmetrical architecture. It is shown that TgPRS does not display extant fold switching, in contrast to P. falciparum PRS, despite having over 65% sequence identity. Finally, structure-comparison analyses suggest the utility of r.m.s.d. per residue (r.m.s.d.(/res)) as a robust tool to detect structural alterations even when the r.m.s.d. is low. Apo TgPRS reveals FF/HF-induced rigidity and this work has implications for drug-design studies that rely on the apo structures of target proteins. | ||
| + | |||
| + | Conformational heterogeneity in apo and drug-bound structures of Toxoplasma gondii prolyl-tRNA synthetase.,Mishra S, Malhotra N, Kumari S, Sato M, Kikuchi H, Yogavel M, Sharma A Acta Crystallogr F Struct Biol Commun. 2019 Nov 1;75(Pt 11):714-724. doi:, 10.1107/S2053230X19014808. Epub 2019 Nov 7. PMID:31702585<ref>PMID:31702585</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6aa0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Proline--tRNA ligase]] | [[Category: Proline--tRNA ligase]] | ||
| + | [[Category: Toxgm]] | ||
[[Category: Kumari, S]] | [[Category: Kumari, S]] | ||
[[Category: Mishra, S]] | [[Category: Mishra, S]] | ||
Revision as of 07:49, 11 March 2020
Crystal Structure of Toxoplasma gondii Prolyl tRNA Synthetase (TgPRS) in Apo Form
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