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Crystallization and preliminary X-ray characterization of the atypical glutaminyl-tRNA synthetase fromDeinococcus radiodurans
- Source :
- Acta Crystallographica Section D: Biological Crystallography, Acta Crystallographica Section D: Biological Crystallography, International Union of Crystallography, 2004, 60 (12), pp.2361-2363. ⟨10.1107/S0907444904026691⟩
- Publication Year :
- 2004
- Publisher :
- International Union of Crystallography (IUCr), 2004.
-
Abstract
- The glutaminyl-tRNA synthetase (GlnRS) from the radiation-resistant bacterium Deinococcus radiodurans differs from known GlnRSs and other tRNA synthetases by the presence of an additional C-terminal domain resembling the C-terminal region of the GatB subunit of tRNA-dependent amidotransferase (AdT). This atypical synthetase was overexpressed in Escherichia coli, purified and crystallized in the presence of PEG 3350. Orthorhombic crystals were obtained that belong to space group P2(1)2(1)2(1) and diffract to 2.3 A resolution. The crystal structure was solved by molecular replacement using the structure of E. coli GlnRS as a search model.
- Subjects :
- Nitrogenous Group Transferases
Protein subunit
030303 biophysics
Crystal structure
Crystallography, X-Ray
medicine.disease_cause
Amino Acyl-tRNA Synthetases
03 medical and health sciences
X-Ray Diffraction
Structural Biology
Escherichia coli
medicine
TRNA aminoacylation
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Molecular replacement
tRNA
030304 developmental biology
Glutamine amidotransferase
0303 health sciences
biology
Deinococcus radiodurans
General Medicine
biology.organism_classification
Protein Structure, Tertiary
Biochemistry
Transfer RNA
Deinococcus
Crystallization
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 60
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section D Biological Crystallography
- Accession number :
- edsair.doi.dedup.....541d5ac3a3423b416b7451ff173cf166
- Full Text :
- https://doi.org/10.1107/s0907444904026691