3NV9
Crystal structure of Entamoeba histolytica Malic Enzyme
3NV9 の概要
| エントリーDOI | 10.2210/pdb3nv9/pdb |
| 分子名称 | Malic enzyme, SULFATE ION, SODIUM ION, ... (6 entities in total) |
| 機能のキーワード | rossmann fold, oxidoreductase |
| 由来する生物種 | Entamoeba histolytica |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 109166.64 |
| 構造登録者 | Dutta, D.,Chakrabarty, A.,Ghosh, S.K.,Das, A.K. (登録日: 2010-07-08, 公開日: 2011-07-20, 最終更新日: 2025-06-25) |
| 主引用文献 | Chakrabarty, A.,Dutta, D.,Baidya, M.,Dutta, A.,Das, A.K.,Ghosh, S.K. Metronidazole Activation by a Deeply Entangled Dimeric Malic Enzyme in Entamoeba histolytica. Pathogens, 14:-, 2025 Cited by PubMed Abstract: Metronidazole is the preferred drug for treating amoebiasis caused by . Its antiamoebic activity is primarily attributed to activation by various reductases. This study reports an alternative activation pathway in mediated by the decarboxylating malic enzyme. Functional characterization of this NADPH-dependent enzyme reveals that it is secreted into the extracellular milieu and may play a role in adhesion to human enteric cells. Structural analysis of the malic enzyme (EhME) demonstrates that the protein forms a strict dimer, with the protomers interlocked by a unique knot structure formed by two polypeptide chains. This distinctive structural feature closely aligns EhME with its prokaryotic counterparts. In conclusion, our findings reveal that harbors a deeply entangled dimeric malic enzyme that contributes to metronidazole susceptibility, sharing structural similarities with bacterial malic enzymes. PubMed: 40137762DOI: 10.3390/pathogens14030277 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.25 Å) |
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