2cv2

File:2cv2.gif

spinqualitylabelsall models 2cv2, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and an enzyme inhibitor, Glu-AMS

OverviewOverview

Glutamyl-tRNA synthetase (GluRS) is one of the aminoacyl-tRNA synthetases, that require the cognate tRNA for specific amino acid recognition and, activation. We analyzed the role of tRNA in amino acid recognition by, crystallography. In the GluRS*tRNA(Glu)*Glu structure, GluRS and tRNA(Glu), collaborate to form a highly complementary L-glutamate-binding site. This, collaborative site is functional, as it is formed in the same manner in, pretransition-state mimic, GluRS*tRNA(Glu)*ATP*Eol (a glutamate analog), and posttransition-state mimic, GluRS*tRNA(Glu)*ESA (a glutamyl-adenylate, analog) structures. In contrast, in the GluRS*Glu structure, only GluRS, forms the amino acid-binding site, which is defective and accounts for the, binding of incorrect amino acids, such as D-glutamate and L-glutamine., Therefore, tRNA(Glu) is essential for formation of the completely, functional binding site for L-glutamate. These structures, together with, our previously described structures, reveal that tRNA plays a crucial role, in accurate positioning of both L-glutamate and ATP, thus driving the, amino acid activation.

About this StructureAbout this Structure

2CV2 is a Single protein structure of sequence from Thermus thermophilus with MG, CL and GSU as ligands. Active as Glutamate--tRNA ligase, with EC number 6.1.1.17 Full crystallographic information is available from OCA.

ReferenceReference

Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase., Sekine S, Shichiri M, Bernier S, Chenevert R, Lapointe J, Yokoyama S, Structure. 2006 Dec;14(12):1791-9. PMID:17161369

Page seeded by OCA on Wed Nov 21 09:16:50 2007