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• W2010919237 startingPage "865" @default.
• W2010919237 abstract "Most dUTP pyrophosphatases (dUTPases) are homotrimers with interfaces formed between subunit surfaces, in the central channel, and by C-terminal beta-strand swapping. Analysis of intersubunit interactions reveals an important cohesive role for the C-terminus. This is reflected in the crystal structure of fruitfly dUTPase displaying a dimeric organization in crystals grown in alcohol solution, where only beta-strand swapping interactions between subunits are retained from the usual trimer structure. Mutations of a suggested hinge proline destabilize human and Escherichia coli dUTPases without preventing trimeric organization. Trimer formation was, however, prevented in the human enzyme by truncating the C-terminus before the swapping arm. The molecular shape of full-length enzymes in solution reveals the localization and variation in flexibility of N- and C-terminal segments." @default.
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• W2010919237 date "2009-02-11" @default.
• W2010919237 modified "2023-10-17" @default.
• W2010919237 title "Molecular shape and prominent role of β-strand swapping in organization of dUTPase oligomers" @default.
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• W2010919237 doi "https://doi.org/10.1016/j.febslet.2009.02.011" @default.
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