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7OL1

The X-ray structure of L-threonine dehydrogenase from the common hospital pathogen Clostridium difficile.

7OL1 の概要
エントリーDOI10.2210/pdb7ol1/pdb
分子名称L-threonine 3-dehydrogenase (2 entities in total)
機能のキーワードdehydrogenase, apoenzyme., oxidoreductase
由来する生物種Clostridioides difficile (Peptoclostridium difficile)
タンパク質・核酸の鎖数2
化学式量合計76416.70
構造登録者
Guo, J.,Cooper, J.B. (登録日: 2021-05-18, 公開日: 2021-06-16, 最終更新日: 2024-01-31)
主引用文献Adjogatse, E.,Bennett, J.,Guo, J.,Erskine, P.T.,Wood, S.P.,Wren, B.W.,Cooper, J.B.
The X-ray structure of L-threonine dehydrogenase from the common hospital pathogen Clostridium difficile.
Acta Crystallogr.,Sect.F, 77:269-274, 2021
Cited by
PubMed Abstract: In many prokaryotes, the first step of threonine metabolism is catalysed by the enzyme threonine dehydrogenase (TDH), which uses NAD to oxidize its substrate to 2-amino-3-ketobutyrate. The absence of a functional TDH gene in humans suggests that inhibitors of this enzyme may have therapeutic potential against pathogens which are reliant on this enzyme. Here, TDH from Clostridium difficile has been cloned and overexpressed, and the X-ray structure of the apoenzyme form has been determined at 2.6 Å resolution.
PubMed: 34341193
DOI: 10.1107/S2053230X21007135
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.6 Å)
構造検証レポート
Validation report summary of 7ol1
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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