1G59

GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).

Summary for 1G59

• Entry DOI: 10.2210/pdb1g59/pdb
• Related: 1GLN
• Descriptor: TRNA(GLU), GLUTAMYL-TRNA SYNTHETASE (3 entities in total)
• Functional Keywords: aminoacyl-trna synthetase, protein-rna complex, transfer rna, riken structural genomics/proteomics initiative, rsgi, structural genomics, ligase-rna complex, ligase/rna
• Biological source: Thermus thermophilus
• Cellular location: Cytoplasm: P27000
• Total number of polymer chains: 4
• Total formula weight: 156170.14

Authors

Sekine, S.,Nureki, O.,Shimada, A.,Vassylyev, D.G.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2000-10-31, release date: 2001-09-01, Last modification date: 2023-08-02)

Primary citation

Sekine, S.,Nureki, O.,Shimada, A.,Vassylyev, D.G.,Yokoyama, S.
Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase.
Nat.Struct.Biol., 8:203-206, 2001

PubMed 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'.

PubMed: 11224561
DOI: 10.1038/84927

Experimental method

X-RAY DIFFRACTION (2.4 Å)