4upa

From Proteopedia

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

Structural highlights

4upa 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 2.901Å
Ligands:
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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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. 2014 Oct 24;588(23):4478-4486. doi: 10.1016/j.febslet.2014.10.019. PMID:25448989 doi:http://dx.doi.org/10.1016/j.febslet.2014.10.019