engleski

The first crystal structure of plant aminoacyl-tRNA synthetase: seryl-tRNA synthetase from Arabidopsis thaliana

Seryl-tRNA synthetase (SerRS) plays essential role in translation process by covalent attachment of serine to its cognate tRNASer. Most SerRS enzymes belong to so called bacterial type that is found in most archea, bacteria and eukaryotes. Small number of enzymes found in methanogenic archea show structural and mechanistic differencies and can be classied as methanogenic type1. Moreover higher eukaryotic SerRS like human SerRS possesses two types of additional insertions: Insertion I (G75-N97) and Insertion II (K253-N261) located in the t-RNA binding domain and in the catalytic core, respectively2. Until now the crystal structure of human SerRS as well as of several prokaryotic systems and lower eukaryote has been studied by X-ray crystallography while no crystallographic structure of any plant SerRS is known to date. In order to clarify the structural and functional properties of plant SerRS (pSerRS) we performed cloning, purification, crystallization and X-ray analysis studies. Crystals shaped like plates were prepared by the sitting drop vapor diffusion method using an automated crystallization platform (Oryx 8 robot). Diffraction data were measured at the XRD1 beamline (Elettra, Trieste, Italy) and were collected to the resolution of 2.8 Å. The crystals belong to the monoclinic space group C2 and the structure of pSerRS has been solved by the molecular replacement method. 1 Bilokapić, S., Maier, T., Ahel, D., Gruić-Sovulj, I., Söll, D., Weygand-Đurašević, I. & Ban, N. (2006). EMBO J. 25, 2498-2509. 2 Xiaoling, X., Yi, S. & Xiang-Lei, Y. (2013). Structure. 21, 2078-2086.

Arabidopsis thaliana; SerRS; crystal structure

nije evidentirano