3ECY

Crystal structural analysis of Drosophila melanogaster dUTPase

3ECY の概要

• エントリーDOI: 10.2210/pdb3ecy/pdb
• 分子名称: CG4584-PA, isoform A (BcDNA.LD08534) (2 entities in total)
• 機能のキーワード: jelly-roll, dimeric assembly, hydrolase
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34707.59

構造登録者

Takacs, E.,Barabas, O.,Vertessy, B.G. (登録日: 2008-09-02, 公開日: 2008-10-07, 最終更新日: 2023-08-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.88 Å)