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5AVO

Crystal structure of the reduced form of homoserine dehydrogenase from Sulfolobus tokodaii.

5AVO の概要
エントリーDOI10.2210/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
Goto, M.,Yoshimune, K.,Kaneko, R. (登録日: 2015-06-25, 公開日: 2015-11-11, 最終更新日: 2024-11-06)
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: 29124164
DOI: 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)
構造検証レポート
Validation report summary of 5avo
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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