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PDBsum entry 1gln
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Aminoacyl-tRNA synthase
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PDB id
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1gln
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References listed in PDB file
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Key reference
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Title
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Architectures of class-Defining and specific domains of glutamyl-Trna synthetase.
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Authors
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O.Nureki,
D.G.Vassylyev,
K.Katayanagi,
T.Shimizu,
S.Sekine,
T.Kigawa,
T.Miyazawa,
S.Yokoyama,
K.Morikawa.
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Ref.
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Science, 1995,
267,
1958-1965.
[DOI no: ]
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PubMed id
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Abstract
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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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