3ECY

Crystal structural analysis of Drosophila melanogaster dUTPase

Summary for 3ECY

• Entry DOI: 10.2210/pdb3ecy/pdb
• Descriptor: CG4584-PA, isoform A (BcDNA.LD08534) (2 entities in total)
• Functional Keywords: jelly-roll, dimeric assembly, hydrolase
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 34707.59

Authors

Takacs, E.,Barabas, O.,Vertessy, B.G. (deposition date: 2008-09-02, release date: 2008-10-07, Last modification date: 2023-08-30)

Primary citation

Takacs, E.,Barabas, O.,Petoukhov, M.V.,Svergun, D.I.,Vertessy, B.G.
Molecular shape and prominent role of beta-strand swapping in organization of dUTPase oligomers.
Febs Lett., 583:865-871, 2009

PubMed 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.

PubMed: 19302784
DOI: 10.1016/j.febslet.2009.02.011

Experimental method

X-RAY DIFFRACTION (1.88 Å)