5AVO
Crystal structure of the reduced form of homoserine dehydrogenase from Sulfolobus tokodaii.
5AVO の概要
| エントリーDOI | 10.2210/pdb5avo/pdb |
| 関連するPDBエントリー | 4YDR |
| 分子名称 | Homoserine dehydrogenase (2 entities in total) |
| 機能のキーワード | reduced form, oxidoreductase |
| 由来する生物種 | Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 66822.99 |
| 構造登録者 | |
| 主引用文献 | Tomonaga, Y.,Kaneko, R.,Goto, M.,Ohshima, T.,Yoshimune, K. Structural insight into activation of homoserine dehydrogenase from the archaeonSulfolobus tokodaiivia reduction. Biochem Biophys Rep, 3:14-17, 2015 Cited by PubMed Abstract: Homoserine dehydrogenase (HSD; 305 amino acid residues) catalyzes an NAD(P)-dependent reversible reaction between l-homoserine and aspartate 4-semialdehyde and is involved in the aspartate pathway. HSD from the hyperthermophilic archaeon was markedly activated (2.5-fold) by the addition of 0.8 mM dithiothreitol. The crystal structure of the homodimer indicated that the activation was caused by cleavage of the disulfide bond formed between two cysteine residues (C303) in the C-terminal regions of the two subunits. PubMed: 29124164DOI: 10.1016/j.bbrep.2015.07.006 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
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