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==Crystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with AMPPNP== | ==Crystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with AMPPNP== | ||
<StructureSection load='4upa' size='340' side='right' caption='[[4upa]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='4upa' size='340' side='right'caption='[[4upa]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4upa]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UPA OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4upa]] 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=4UPA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4UPA FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.901Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</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=4upa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upa OCA], [https://pdbe.org/4upa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4upa RCSB], [https://www.ebi.ac.uk/pdbsum/4upa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4upa 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;"> | |||
== Publication Abstract from PubMed == | |||
The 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<ref>PMID:25448989</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4upa" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Aminoacyl tRNA synthetase 3D structures|Aminoacyl tRNA synthetase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Entamoeba histolytica]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Bonnefond L]] | ||
[[Category: | [[Category: Nureki O]] | ||
Latest revision as of 13:32, 10 January 2024
Crystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with AMPPNPCrystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with AMPPNP
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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