A three-dimensional structure model of the complex of glutamyl-tRNA synthetase and its cognate tRNA.
A docking model of glutamyl-tRNA synthetase (GluRS) and tRNAGlu was constructed, on the basis of the distinguished similarity between the X-ray crystallographic three-dimensional structures of the N-terminal halves of the Thermus thermophilus GluRS in the free state and the Escherichia coli glutaminyl-tRNA synthetase in a complex with tRNAGln. The modeled structure is energetically favorable and is also well consistent with the results of site-directed mutagenesis studies. The model indicates that the GluRS-specific insertions 2 and 3 fit and bind to the acceptor stem and the D arm, respectively, of the cognate tRNA without affecting other contacts. In particular, insertion 3 strongly interacts with the two D-stem base pairs that are essential for the tRNA-GluRS recognition.
Tateno
M
M
Department of Biophysics and Biochemistry, School of Science, University of Tokyo, Japan.
Nureki
O
O
Sekine
S
S
Kaneda
K
K
Go
M
M
Yokoyama
S
S
D000926:Anticodon; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology; D005975:Glutamate-tRNA Ligase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D009690:Nucleic Acid Conformation; D012352:RNA, Transfer, Glu / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013816:Thermodynamics; D016963:Thermus thermophilus / Q000201:enzymology
D000926:Anticodon; D012352:RNA, Transfer, Glu; D005975:Glutamate-tRNA Ligase