1gln

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{{STRUCTURE_1gln| PDB=1gln | SCENE= }}
{{STRUCTURE_1gln| PDB=1gln | SCENE= }}
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'''ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE'''
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===ARCHITECTURES OF CLASS-DEFINING AND SPECIFIC DOMAINS OF GLUTAMYL-TRNA SYNTHETASE===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 7701318 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7701318}}
==About this Structure==
==About this Structure==
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[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
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Revision as of 02:29, 1 July 2008

Image:1gln.png

Template:STRUCTURE 1gln

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

Template:ABSTRACT PUBMED 7701318

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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