2VIM
X-ray structure of Fasciola hepatica thioredoxin
2VIM の概要
| エントリーDOI | 10.2210/pdb2vim/pdb |
| 分子名称 | THIOREDOXIN (2 entities in total) |
| 機能のキーワード | thioredoxin, trx, thioredoxin fold, oxidoreductase |
| 由来する生物種 | FASCIOLA HEPATICA (LIVER FLUKE) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 11700.44 |
| 構造登録者 | Line, K.,Isupov, M.N.,Garcia-Rodriguez, E.,Maggioli, G.,Parra, F.,Littlechild, J.A. (登録日: 2007-12-05, 公開日: 2008-07-29, 最終更新日: 2024-10-16) |
| 主引用文献 | Line, K.,Isupov, M.N.,Garcia-Rodriguez, E.,Maggioli, G.,Parra, F.,Littlechild, J.A. The Fasciola Hepatica Thioredoxin: High Resolution Structure Reveals Two Oxidation States. Mol.Biochem.Parasitol., 161:44-, 2008 Cited by PubMed Abstract: The Fasciola hepatica thioredoxin protein structure has been determined to 1.45A resolution. This is the first example of a single crystal structure to show the active site cysteine residues in both the reduced and disulfide oxidised form. Consistent with this observation the process of oxidation appears to require very little rearrangement of the surrounding protein structure. The F. hepatica thioredoxin structure has been compared to other thioredoxin protein structures already known and is found to be highly conserved. The F. hepatica protein is most similar to that of the thioredoxin from its human and animal hosts but it resembles other parasitic thioredoxins with regard to having no additional cysteine residues and is therefore not regulated by transient disulfide bond formation as proposed for thioredoxins from higher eukaryotic species. PubMed: 18620002DOI: 10.1016/J.MOLBIOPARA.2008.06.009 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.38 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






