3ecy
From Proteopedia
Crystal structural analysis of Drosophila melanogaster dUTPase
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedMost 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. Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers.,Takacs E, Barabas O, Petoukhov MV, Svergun DI, Vertessy BG FEBS Lett. 2009 Mar 4;583(5):865-71. Epub 2009 Feb 11. PMID:19302784[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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