2cv2: Difference between revisions

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[[Image:2cv2.gif|left|200px]]
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{{STRUCTURE_2cv2|  PDB=2cv2  |  SCENE=  }}  
{{STRUCTURE_2cv2|  PDB=2cv2  |  SCENE=  }}  


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




==Overview==
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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.
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{{ABSTRACT_PUBMED_17161369}}


==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 01:53:52 2008''

Revision as of 22:54, 28 July 2008

File:2cv2.png

Template:STRUCTURE 2cv2

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

Template:ABSTRACT PUBMED 17161369

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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