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2dxi

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(New page: 200px<br /><applet load="2dxi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dxi, resolution 2.20&Aring;" /> '''2.2 A crystal struct...)
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Revision as of 07:43, 21 November 2007

Image:2dxi.gif

2dxi, resolution 2.20Å

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2.2 A crystal structure of glutamyl-tRNA synthetase from Thermus thermophilus complexed with tRNA(Glu), ATP, and L-glutamol

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

2DXI is a Single protein structure of sequence from Thermus thermophilus with MG, ATP and GAU as ligands. Active as Glutamate--tRNA ligase, with EC number 6.1.1.17 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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