Publication Date:
1995-03-31
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nureki, O -- Vassylyev, D G -- Katayanagi, K -- Shimizu, T -- Sekine, S -- Kigawa, T -- Miyazawa, T -- Yokoyama, S -- Morikawa, K -- New York, N.Y. -- Science. 1995 Mar 31;267(5206):1958-65.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics and Biochemistry, School of Science, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7701318" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Amino Acyl-tRNA Synthetases/chemistry
;
Anticodon
;
Biological Evolution
;
Computer Graphics
;
Crystallography, X-Ray
;
Escherichia coli/enzymology
;
Glutamate-tRNA Ligase/*chemistry/metabolism
;
Models, Molecular
;
Molecular Sequence Data
;
Mutagenesis, Site-Directed
;
Protein Conformation
;
Protein Folding
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
RNA, Transfer, Glu/chemistry/metabolism
;
Sequence Alignment
;
Thermus thermophilus/*enzymology
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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