2dxi: Difference between revisions

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==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.

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==

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[[Category: Single protein]]

[[Category: Thermus thermophilus]]

[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]

[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]

[[Category: Sekine, S.]]

[[Category: Yokoyama, S.]]

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[[Category: structural genomics]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Thermus thermophilus]]
-[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
+[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
 [[Category: Sekine, S.]]
 [[Category: Yokoyama, S.]]
@@ Line 28: / Line 28: @@
 [[Category: structural genomics]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:48:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:03:45 2008''