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Crystal structures of Entamoeba histolytica lysyl‐tRNA synthetase reveal conformational changes upon lysine binding and a specific helix bundle domain
Author(s) -
Bonnefond Luc,
Castro de Moura Manuel,
Ribas de Pouplana Lluis,
Nureki Osamu
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.10.019
Subject(s) - entamoeba histolytica , lysine , biochemistry , transfer rna , aminoacyl trna synthetase , entamoeba , adenylate kinase , enzyme , biology , chemistry , amino acid , rna , microbiology and biotechnology , gene
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.