Crystallization and preliminary crystallographic studies of putative threonyl-tRNA synthetases from<i>Aeropyrum pernix</i>and<i>Sulfolobus tokodaii</i>
説明
Threonyl-tRNA synthetase (ThrRS) plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr) and editing misacylation. ThrRS generally contains an N-terminal editing domain, a catalytic domain and an anticodon-binding domain. The sequences of the editing domain in ThrRSs from archaea differ from those in bacteria and eukaryotes. Furthermore, several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the catalytic or the editing domain of ThrRS. To reveal the structural basis for this evolutionary divergence, the two types of ThrRS from the crenarchaea A. pernix and S. tokodaii have been overexpressed in Eschericha coli, purified and crystallized by the hanging-drop vapour-diffusion method. Diffraction data were collected and the structure of a selenomethionine-labelled A. pernix type-1 ThrRS crystal has been solved using the MAD method.
収録刊行物
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- Acta Crystallographica Section F Structural Biology and Crystallization Communications
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Acta Crystallographica Section F Structural Biology and Crystallization Communications 64 903-910, 2008-09-30
International Union of Crystallography (IUCr)
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キーワード
- MESH: Threonine-tRNA Ligase
- Models, Molecular
- [SDV.BIBS] Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]
- Protein Conformation
- Archaeal Proteins
- MESH: Amino Acid Sequence
- MESH: Archaeal Proteins
- Aeropyrum
- MESH: Crystallography, X-Ray
- Crystallography, X-Ray
- [SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]
- Sulfolobus
- MESH: Protein Conformation
- Species Specificity
- MESH: Aeropyrum
- MESH: Sulfolobus
- Threonine-tRNA Ligase
- MESH: Species Specificity
- Amino Acid Sequence
- Crystallization
- MESH: Models, Molecular
- MESH: Crystallization