The crystal structure of Trypanosoma cruzi dUTPase reveals a novel dUTP/dUDP binding fold.

Journal article

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 ...

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Authors: Harkiolaki, M; Dodson, E; Bernier-Villamor, V; Turkenburg, J; González-Pacanowska, D

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 12
• Issue: 1
• Pages: 41-53
• Publication date: 2004-01-01
• DOI: 10.1016/j.str.2003.11.016
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Protein Structure, Quaternary; Humans; Crystallography, X-Ray; Dimerization; Binding Sites; Enzyme Inhibitors; Pyrophosphatases; Animals; Protein Binding; Trypanosoma cruzi; Molecular Sequence Data; Amino Acid Sequence; Deoxyuracil Nucleotides; Magnesium