4upa: Difference between revisions
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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=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4up7|4up7]], [[4up8|4up8]], [[4up9|4up9]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4up7|4up7]], [[4up8|4up8]], [[4up9|4up9]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysine--tRNA_ligase Lysine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.6 6.1.1.6] </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=4upa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upa OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4upa RCSB], [http://www.ebi.ac.uk/pdbsum/4upa 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=4upa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4upa OCA], [http://pdbe.org/4upa PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4upa RCSB], [http://www.ebi.ac.uk/pdbsum/4upa PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4upa ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4upa" style="background-color:#fffaf0;"></div> | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 04:19, 19 January 2017
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
Publication 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. References
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