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Tyrosyl-tRNA synthetase: the first crystallization of a human mitochondrial aminoacyl-tRNA synthetase
- Source :
- Acta Crystallograph Sect F Struct Biol Cryst Commun, Acta Crystallograph Sect F Struct Biol Cryst Commun, 2007, 63 (Pt 4), pp.338-41. ⟨10.1107/S1744309107012481⟩
- Publication Year :
- 2007
- Publisher :
- HAL CCSD, 2007.
-
Abstract
- International audience; Human mitochondrial tyrosyl-tRNA synthetase and a truncated version with its C-terminal S4-like domain deleted were purified and crystallized. Only the truncated version, which is active in tyrosine activation and Escherichia coli tRNA(Tyr) charging, yielded crystals suitable for structure determination. These tetragonal crystals, belonging to space group P4(3)2(1)2, were obtained in the presence of PEG 4000 as a crystallizing agent and diffracted X-rays to 2.7 A resolution. Complete data sets could be collected and led to structure solution by molecular replacement.
- Subjects :
- MESH: DNA Primers
Protein Conformation
MESH: Mitochondria
Biophysics
Biology
Mitochondrion
MESH: Base Sequence
Crystallography, X-Ray
010402 general chemistry
medicine.disease_cause
01 natural sciences
Biochemistry
03 medical and health sciences
chemistry.chemical_compound
Protein structure
MESH: Protein Conformation
Tyrosine-tRNA Ligase
Structural Biology
MESH: Tyrosine-tRNA Ligase
Genetics
medicine
Humans
Molecular replacement
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
Tyrosine
Escherichia coli
DNA Primers
030304 developmental biology
MESH: Crystallization
0303 health sciences
MESH: Humans
Base Sequence
Aminoacyl tRNA synthetase
Condensed Matter Physics
MESH: Crystallography, X-Ray
Mitochondria
0104 chemical sciences
enzymes and coenzymes (carbohydrates)
Tyrosine—tRNA ligase
chemistry
Crystallization Communications
Transfer RNA
Crystallization
hormones, hormone substitutes, and hormone antagonists
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Acta Crystallograph Sect F Struct Biol Cryst Commun, Acta Crystallograph Sect F Struct Biol Cryst Commun, 2007, 63 (Pt 4), pp.338-41. ⟨10.1107/S1744309107012481⟩
- Accession number :
- edsair.doi.dedup.....5b5ecd17e8583e11f820863055e8159f