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1gln

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(New page: 200px<br /><applet load="1gln" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gln, resolution 2.5&Aring;" /> '''ARCHITECTURES OF CLAS...)
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[[Image:1gln.gif|left|200px]]<br /><applet load="1gln" size="350" color="white" frame="true" align="right" spinBox="true"
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caption="1gln, resolution 2.5&Aring;" />
'''ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE'''<br />
'''ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE'''<br />
==Overview==
==Overview==
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The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and, refined at 2.5 A resolution. The amino-terminal half of GluRS shows a, geometrical similarity with that of Escherichia coli glutaminyl-tRNA, synthetase (GlnRS) of the same subclass in class I, comprising the class, I-specific Rossmann fold domain and the intervening subclass-specific, alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific, recognition of the D and acceptor stems of tRNA(Glu) as indicated by, mutagenesis analyses based on the docking properties of GluRS and tRNA. In, striking contrast to the beta-barrel structure of the GlnRS, carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an, all-alpha-helix architecture, an alpha-helix cage, and mutagenesis, analyses indicated that it had a role in the anticodon recognition.
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The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.
==About this Structure==
==About this Structure==
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1GLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GLN OCA].
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1GLN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GLN OCA].
==Reference==
==Reference==
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[[Category: Morikawa, K.]]
[[Category: Morikawa, K.]]
[[Category: Nureki, O.]]
[[Category: Nureki, O.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Sekine, S.]]
[[Category: Sekine, S.]]
[[Category: Shimizu, T.]]
[[Category: Shimizu, T.]]
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[[Category: Vassylyev, D.G.]]
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[[Category: Vassylyev, D G.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
[[Category: riken structural genomics/proteomics initiative]]
[[Category: riken structural genomics/proteomics initiative]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:09:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:25 2008''

Revision as of 10:51, 21 February 2008


1gln, resolution 2.5Å

Drag the structure with the mouse to rotate

ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE

Overview

The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus, was solved and refined at 2.5 A resolution. The amino-terminal half of GluRS shows a geometrical similarity with that of Escherichia coli glutaminyl-tRNA synthetase (GlnRS) of the same subclass in class I, comprising the class I-specific Rossmann fold domain and the intervening subclass-specific alpha/beta domain. These domains were found to have two GluRS-specific, secondary-structure insertions, which then participated in the specific recognition of the D and acceptor stems of tRNA(Glu) as indicated by mutagenesis analyses based on the docking properties of GluRS and tRNA. In striking contrast to the beta-barrel structure of the GlnRS carboxyl-terminal half, the GluRS carboxyl-terminal half displayed an all-alpha-helix architecture, an alpha-helix cage, and mutagenesis analyses indicated that it had a role in the anticodon recognition.

About this Structure

1GLN is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Architectures of class-defining and specific domains of glutamyl-tRNA synthetase., Nureki O, Vassylyev DG, Katayanagi K, Shimizu T, Sekine S, Kigawa T, Miyazawa T, Yokoyama S, Morikawa K, Science. 1995 Mar 31;267(5206):1958-65. PMID:7701318

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