1gln

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gln FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gln OCA], [http://www.ebi.ac.uk/pdbsum/1gln PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gln RCSB]</span>
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:46:37 2008''

Revision as of 17:46, 30 March 2008

Image:1gln.gif


PDB ID 1gln

Drag the structure with the mouse to rotate
, resolution 2.5Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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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