4up7

Crystal structure of Entamoeba histolytica lysyl-tRNA synthetase in complex with lysyl-adenylate

spinqualitylabelsall models 4up7, resolution 2.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4up7 is a 1 chain structure with sequence from Entamoeba histolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.789Å Ligands: LAD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4M7X2_ENTH1 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aminoacyl tRNA synthetase 3D structures

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