Summary information and primary citation
- PDB-id
-
1g59;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- ligase-RNA
- Method
- X-ray (2.4 Å)
- Summary
- Glutamyl-trna synthetase complexed with trna(glu).
- Reference
-
Sekine S, Nureki O, Shimada A, Vassylyev DG, Yokoyama S
(2001): "Structural
basis for anticodon recognition by discriminating
glutamyl-tRNA synthetase." Nat.Struct.Biol.,
8, 203-206. doi: 10.1038/84927.
- Abstract
- Glutamyl-tRNA synthetases (GluRSs) are divided into two
distinct types, with regard to the presence or absence of
glutaminyl-tRNA synthetase (GlnRS) in the genetic
translation systems. In the original 19-synthetase systems
lacking GlnRS, the 'non-discriminating' GluRS glutamylates
both tRNAGlu and tRNAGln. In contrast, in the evolved
20-synthetase systems with GlnRS, the 'discriminating'
GluRS aminoacylates only tRNAGlu. Here we report the 2.4 A
resolution crystal structure of a 'discriminating'
GluRS.tRNAGlu complex from Thermus thermophilus. The GluRS
recognizes the tRNAGlu anticodon bases via two
alpha-helical domains, maintaining the base stacking. We
show that the discrimination between the Glu and Gln
anticodons (34YUC36 and 34YUG36, respectively) is achieved
by a single arginine residue (Arg 358). The mutation of Arg
358 to Gln resulted in a GluRS that does not discriminate
between the Glu and Gln anticodons. This change mimics the
reverse course of GluRS evolution from anticodon
'non-dicsriminating' to 'discriminating'.
