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8bhd
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==N-terminal domain of Plasmodium berghei glutamyl-tRNA synthetase (Tbxo4 derivative crystal structure)== | |
| + | <StructureSection load='8bhd' size='340' side='right'caption='[[8bhd]], [[Resolution|resolution]] 3.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8bhd]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Plasmodium_berghei_ANKA Plasmodium berghei ANKA]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8BHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8BHD FirstGlance]. <br> | ||
| + | </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=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TB:TERBIUM(III)+ION'>TB</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=8bhd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8bhd OCA], [https://pdbe.org/8bhd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8bhd RCSB], [https://www.ebi.ac.uk/pdbsum/8bhd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8bhd ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A509AR09_PLABA A0A509AR09_PLABA] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | tRip is a tRNA import protein specific to Plasmodium, the causative agent of malaria. In addition to its membrane localization and tRNA trafficking properties, tRip has the capacity to associate with three aminoacyl-tRNA synthetases (aaRS), the glutamyl- (ERS), glutaminyl- (QRS), and methionyl- (MRS) tRNA synthetases. In eukaryotes, such multi-aaRSs complexes (MSC) regulate the moonlighting activities of aaRSs. In Plasmodium, tRip and the three aaRSs all contain an N-terminal GST-like domain involved in the assembly of two independent complexes: the Q-complex (tRip:ERS:QRS) and the M-complex (tRip:ERS:MRS) with a 2:2:2 stoichiometry and in which the association of the GST-like domains of tRip and ERS (tRip-N:ERS-N) is central. In this study, the crystal structure of the N-terminal GST-like domain of ERS was solved and made possible further investigation of the solution architecture of the Q- and M-complexes by small-angle X-ray scattering (SAXS). This strategy relied on the engineering of a tRip-N-ERS-N chimeric protein to study the structural scaffold of both Plasmodium MSCs and confirm the unique homodimerization pattern of tRip in solution. The biological impact of these structural arrangements is discussed. This article is protected by copyright. All rights reserved. | ||
| - | + | Solution x-ray scattering highlights discrepancies in Plasmodium multi-aminoacyl-tRNA synthetase complexes.,Jaramillo Ponce JR, Theobald-Dietrich A, Benas P, Paulus C, Sauter C, Frugier M Protein Sci. 2023 Jan 6:e4564. doi: 10.1002/pro.4564. PMID:36606712<ref>PMID:36606712</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8bhd" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Plasmodium berghei ANKA]] | ||
| + | [[Category: Benas P]] | ||
| + | [[Category: Frugier M]] | ||
| + | [[Category: Jaramillo Ponce JR]] | ||
| + | [[Category: Legrand P]] | ||
| + | [[Category: Sauter C]] | ||
Current revision
N-terminal domain of Plasmodium berghei glutamyl-tRNA synthetase (Tbxo4 derivative crystal structure)
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