4UP7

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

Summary for 4UP7

• Entry DOI: 10.2210/pdb4up7/pdb
• Related: 4UP8 4UP9 4UPA
• Descriptor: LYSINE--TRNA LIGASE, ADENOSINE-5'-[LYSYL-PHOSPHATE] (2 entities in total)
• Functional Keywords: ligase, aminoacylation
• Biological source: ENTAMOEBA HISTOLYTICA
• Total number of polymer chains: 1
• Total formula weight: 88216.61

Authors

Bonnefond, L.,Nureki, O. (deposition date: 2014-06-14, release date: 2014-10-29, Last modification date: 2024-01-10)

Primary citation

Bonnefond, L.,Castro De Moura, M.,Ribas De Pouplana, L.,Nureki, O.
Crystal Structures of Entamoeba Histolytica Lysyl-tRNA Synthetase Reveal Conformational Changes Upon Lysine Binding and a Specific Helix Bundle Domain.
FEBS Lett., 588:4478-, 2014

PubMed Abstract: 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.

PubMed: 25448989
DOI: 10.1016/J.FEBSLET.2014.10.019

Experimental method

X-RAY DIFFRACTION (2.789 Å)