2cv2

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spinqualitylabelsall models PDB ID 2cv2 Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.69Å
Ligands:	, and
Activity:	Glutamate--tRNA ligase, with EC number 6.1.1.17
Coordinates:	save as pdb, mmCIF, xml

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

Overview

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 Structure

2CV2 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

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

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