4up7: Difference between revisions
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<StructureSection load='4up7' size='340' side='right'caption='[[4up7]], [[Resolution|resolution]] 2.79Å' scene=''> | <StructureSection load='4up7' size='340' side='right'caption='[[4up7]], [[Resolution|resolution]] 2.79Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4up7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4up7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Entamoeba_histolytica Entamoeba histolytica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UP7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LAD:ADENOSINE-5-[LYSYL-PHOSPHATE]'>LAD</scene | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LAD:ADENOSINE-5-[LYSYL-PHOSPHATE]'>LAD</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=4up7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4up7 OCA], [https://pdbe.org/4up7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4up7 RCSB], [https://www.ebi.ac.uk/pdbsum/4up7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4up7 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/C4M7X2_ENTH1 C4M7X2_ENTH1] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 25: | Line 25: | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Entamoeba histolytica]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bonnefond L]] | |||
[[Category: Bonnefond | [[Category: Nureki O]] | ||
[[Category: Nureki | |||
Revision as of 10:30, 29 March 2023
Crystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylateCrystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylate
Structural highlights
FunctionPublication Abstract from PubMedThe class II lysyl-tRNA synthetases (KRS) are conserved aminoacyl-tRNA synthetases that attach lysine to the cognate tRNA in a two-step mechanism. The enzyme from the parasitic protozoan Entamoeba histolytica was crystallized in the presence of small ligands to generate snapshots of the lysine-adenylate formation. The residues involved in lysine activation are highly conserved and the active site closes around the lysyl-adenylate, as observed in bacterial KRS. The Entamoeba EMAPII-like polypeptide is not resolved in the crystals, but another Entamoeba-specific insertion could be modeled as a small helix bundle that may contribute to tRNA binding through interaction with the tRNA hinge. Crystal structures of Entamoeba histolytica lysyl-tRNA synthetase reveal conformational changes upon lysine binding and a specific helix bundle domain.,Bonnefond L, Castro de Moura M, Ribas de Pouplana L, Nureki O FEBS Lett. 2014 Oct 24;588(23):4478-4486. doi: 10.1016/j.febslet.2014.10.019. PMID:25448989[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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