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| {{STRUCTURE_2cv0| PDB=2cv0 | SCENE= }} | | {{STRUCTURE_2cv0| PDB=2cv0 | SCENE= }} |
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| '''Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and L-glutamate'''
| | ===Glutamyl-tRNA synthetase from Thermus thermophilus in complex with tRNA(Glu) and L-glutamate=== |
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| ==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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17161369}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17161369 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17161369}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Rsgi]] | | [[Category: Rsgi]] |
| [[Category: Structural genomic]] | | [[Category: Structural genomic]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:07:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:31:01 2008'' |