1DUP

DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDO HYDROLASE (D-UTPASE)

1DUP の概要

• エントリーDOI: 10.2210/pdb1dup/pdb
• 分子名称: DEOXYURIDINE 5'-TRIPHOSPHATE NUCLEOTIDOHYDROLASE (2 entities in total)
• 機能のキーワード: hydrolase, nucleotide metabolism
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16302.61

構造登録者

Dauter, Z.,Wilson, K.S.,Larsson, G.,Nyman, P.O.,Cedergren, E. (登録日: 1995-09-01, 公開日: 1995-11-14, 最終更新日: 2024-02-07)

主引用文献

Cedergren-Zeppezauer, E.S.,Larsson, G.,Nyman, P.O.,Dauter, Z.,Wilson, K.S.
Crystal structure of a dUTPase.
Nature, 355:740-743, 1992

PubMed Abstract: The enzyme dUTPase catalyses the hydrolysis of dUTP and maintains a low intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. dUTPase from Escherichia coli is strictly specific for its dUTP substrate, the active site discriminating between nucleotides with respect to the sugar moiety as well as the pyrimidine base. Here we report the three-dimensional structure of E. coli dUTPase determined by X-ray crystallography at a resolution of 1.9 A. The enzyme is a symmetrical trimer, and of the 152 amino acid residues in the subunit, the first 136 are visible in the crystal structure. The tertiary structure resembles a jelly-roll fold and does not show the 'classical' nucleotide-binding domain. In the quaternary structure there is a complex interaction between the subunits that may be important in catalysis. This possibility is supported by the location of conserved elements in the sequence.

PubMed: 1311056
DOI: 10.1038/355740a0

実験手法

X-RAY DIFFRACTION (1.9 Å)