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DOI | 10.2210/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 | |
| 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: 34341193DOI: 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) |
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