2IWT
Thioredoxin h2 (HvTrxh2) in a mixed disulfide complex with the target protein BASI
2IWT の概要
| エントリーDOI | 10.2210/pdb2iwt/pdb |
| 関連するPDBエントリー | 1AVA |
| 分子名称 | THIOREDOXIN H ISOFORM 2, ALPHA-AMYLASE/SUBTILISIN INHIBITOR, CITRATE ANION, ... (4 entities in total) |
| 機能のキーワード | protease inhibitor, disulfide reductase, basi, amy2, redox, thioredoxin, oxidoreductase, substrate recognition, disulfide intermediate, alpha-amylase inhibitor, serine protease inhibitor |
| 由来する生物種 | HORDEUM VULGARE (BARLEY) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 34747.14 |
| 構造登録者 | Maeda, K.,Hagglund, P.,Finnie, C.,Svensson, B.,Henriksen, A. (登録日: 2006-07-04, 公開日: 2006-11-15, 最終更新日: 2024-10-16) |
| 主引用文献 | Maeda, K.,Hagglund, P.,Finnie, C.,Svensson, B.,Henriksen, A. Structural Basis for Target Protein Recognition by the Protein Disulfide Reductase Thioredoxin. Structure, 14:1701-, 2006 Cited by PubMed Abstract: Thioredoxin is ubiquitous and regulates various target proteins through disulfide bond reduction. We report the structure of thioredoxin (HvTrxh2 from barley) in a reaction intermediate complex with a protein substrate, barley alpha-amylase/subtilisin inhibitor (BASI). The crystal structure of this mixed disulfide shows a conserved hydrophobic motif in thioredoxin interacting with a sequence of residues from BASI through van der Waals contacts and backbone-backbone hydrogen bonds. The observed structural complementarity suggests that the recognition of features around protein disulfides plays a major role in the specificity and protein disulfide reductase activity of thioredoxin. This novel insight into the function of thioredoxin constitutes a basis for comprehensive understanding of its biological role. Moreover, comparison with structurally related proteins shows that thioredoxin shares a mechanism with glutaredoxin and glutathione transferase for correctly positioning substrate cysteine residues at the catalytic groups but possesses a unique structural element that allows recognition of protein disulfides. PubMed: 17098195DOI: 10.1016/J.STR.2006.09.012 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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