2HZ7

Crystal structure of the Glutaminyl-tRNA synthetase from Deinococcus radiodurans

Summary for 2HZ7

• Entry DOI: 10.2210/pdb2hz7/pdb
• Descriptor: Glutaminyl-tRNA synthetase (2 entities in total)
• Functional Keywords: rossmann fold, glnrs core, class i aminoacyl-trna synthetase, ligase
• Biological source: Deinococcus radiodurans
• Cellular location: Cytoplasm : P56926
• Total number of polymer chains: 1
• Total formula weight: 93460.67

Authors

Deniziak, M.,Sauter, C.,Becker, H.D.,Paulus, C.,Giege, R.,Kern, D. (deposition date: 2006-08-08, release date: 2007-04-24, Last modification date: 2023-08-30)

Primary citation

Deniziak, M.,Sauter, C.,Becker, H.D.,Paulus, C.A.,Giege, R.,Kern, D.
Deinococcus glutaminyl-tRNA synthetase is a chimer between proteins from an ancient and the modern pathways of aminoacyl-tRNA formation
Nucleic Acids Res., 35:1421-1431, 2007

PubMed Abstract: Glutaminyl-tRNA synthetase from Deinococcus radiodurans possesses a C-terminal extension of 215 residues appending the anticodon-binding domain. This domain constitutes a paralog of the Yqey protein present in various organisms and part of it is present in the C-terminal end of the GatB subunit of GatCAB, a partner of the indirect pathway of Gln-tRNA(Gln) formation. To analyze the peculiarities of the structure-function relationship of this GlnRS related to the Yqey domain, a structure of the protein was solved from crystals diffracting at 2.3 A and a docking model of the synthetase complexed to tRNA(Gln) constructed. The comparison of the modeled complex with the structure of the E. coli complex reveals that all residues of E. coli GlnRS contacting tRNA(Gln) are conserved in D. radiodurans GlnRS, leaving the functional role of the Yqey domain puzzling. Kinetic investigations and tRNA-binding experiments of full length and Yqey-truncated GlnRSs reveal that the Yqey domain is involved in tRNA(Gln) recognition. They demonstrate that Yqey plays the role of an affinity-enhancer of GlnRS for tRNA(Gln) acting only in cis. However, the presence of Yqey in free state in organisms lacking GlnRS, suggests that this domain may exert additional cellular functions.

PubMed: 17284460
DOI: 10.1093/nar/gkl1164

Experimental method

X-RAY DIFFRACTION (2.3 Å)