1OGK
The crystal structure of Trypanosoma cruzi dUTPase in complex with dUDP
1OGK の概要
| エントリーDOI | 10.2210/pdb1ogk/pdb |
| 関連するPDBエントリー | 1OGL |
| 分子名称 | DEOXYURIDINE TRIPHOSPHATASE, DEOXYURIDINE-5'-DIPHOSPHATE (2 entities in total) |
| 機能のキーワード | dimer, hydrolase |
| 由来する生物種 | TRYPANOSOMA CRUZI |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 129581.85 |
| 構造登録者 | Harkiolaki, M.,Dodson, E.J.,Bernier-Villamor, V.,Turkenburg, J.P.,Gonzalez-Pacanowska, D.,Wilson, K.S. (登録日: 2003-05-07, 公開日: 2004-01-22, 最終更新日: 2024-05-01) |
| 主引用文献 | Harkiolaki, M.,Dodson, E.J.,Bernier-Villamor, V.,Turkenburg, J.P.,Gonzalez-Pacanowska, D.,Wilson, K.S. The Crystal Structure of Trypanosoma Cruzi Dutpase Reveals a Novel Dutp/Dudp Binding Fold Structure, 12:41-, 2004 Cited by PubMed Abstract: dUTPase is an essential enzyme involved with nucleotide metabolism and replication. We report here the X-ray structure of Trypanosoma cruzi dUTPase in its native conformation and as a complex with dUDP. These reveal a novel protein fold that displays no structural similarities to previously described dUTPases. The molecular unit is a dimer with two active sites. Nucleotide binding promotes extensive structural rearrangements, secondary structure remodeling, and rigid body displacements of 20 A or more, which effectively bury the substrate within the enzyme core for the purpose of hydrolysis. The molecular complex is a trapped enzyme-substrate arrangement which clearly demonstrates structure-induced specificity and catalytic potential. This enzyme is a novel dUTPase and therefore a potential drug target in the treatment of Chagas' disease. PubMed: 14725764DOI: 10.1016/J.STR.2003.11.016 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.85 Å) |
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