3KH4
Crystal structure of human Cu/Zn superoxide dismutase recombinantly produced in Leishmania tarantolae; P6522 crystal form containing 6 chains in the asymmetric unit
3KH4 の概要
| エントリーDOI | 10.2210/pdb3kh4/pdb |
| 関連するPDBエントリー | 3KH3 |
| 分子名称 | Superoxide dismutase [Cu-Zn], COPPER (II) ION, ZINC ION (3 entities in total) |
| 機能のキーワード | eukaryotic expression, leishmania tarantolae, amyotrophic lateral sclerosis, antioxidant, disease mutation, disulfide bond, metal-binding, neurodegeneration, oxidoreductase, phosphoprotein |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cytoplasm: P00441 |
| タンパク質・核酸の鎖数 | 6 |
| 化学式量合計 | 95739.10 |
| 構造登録者 | |
| 主引用文献 | Gazdag, E.M.,Cirstea, I.C.,Breitling, R.,Lukes, J.,Blankenfeldt, W.,Alexandrov, K. Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae. Acta Crystallogr.,Sect.F, 66:871-877, 2010 Cited by PubMed Abstract: The rapid and inexpensive production of high-quality eukaryotic proteins in recombinant form still remains a challenge in structural biology. Here, a protein-expression system based on the protozoan Leishmania tarentolae was used to produce human Cu/Zn superoxide dismutase (SOD1) in recombinant form. Sequential integration of the SOD1 expression cassettes was demonstrated to lead to a linear increase in expression levels to up to 30 mg per litre. Chromatographic purification resulted in 90% pure recombinant protein, with a final yield of 6.5 mg per litre of culture. The protein was crystallized and the structures of two new crystal forms were determined. These results demonstrate the suitability of the L. tarentolae expression system for structural research. PubMed: 20693657DOI: 10.1107/S1744309110019330 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.5 Å) |
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