1SEH

Crystal structure of E. coli dUTPase complexed with the product dUMP

1SEH の概要

• エントリーDOI: 10.2210/pdb1seh/pdb
• 関連するPDBエントリー: 1RN8 1RNJ 1RO1 1SYL
• 分子名称: Deoxyuridine 5'-triphosphate nucleotidohydrolase, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (4 entities in total)
• 機能のキーワード: enzyme-ligand complex, jelly roll, hydrolase
• 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: 16732.94

構造登録者

Barabas, O.,Kovari, J.,Pongracz, V.,Wilmanns, M.,Vertessy, B.G. (登録日: 2004-02-17, 公開日: 2004-09-07, 最終更新日: 2023-10-25)

主引用文献

Barabas, O.,Pongracz, V.,Kovari, J.,Wilmanns, M.,Vertessy, B.G.
Structural Insights into the Catalytic Mechanism of Phosphate Ester Hydrolysis by dUTPase
J.Biol.Chem., 279:42907-42915, 2004

PubMed Abstract: dUTPase is essential to keep uracil out of DNA. Crystal structures of substrate (dUTP and alpha,beta-imino-dUTP) and product complexes of wild type and mutant dUTPases were determined to reveal how an enzyme responsible for DNA integrity functions. A kinetic analysis of wild type and mutant dUTPases was performed to obtain relevant mechanistic information in solution. Substrate hydrolysis is shown to be initiated via in-line nucleophile attack of a water molecule oriented by an activating conserved aspartate residue. Substrate binding in a catalytically competent conformation is achieved by (i) multiple interactions of the triphosphate moiety with catalysis-assisting Mg2+, (ii) a concerted motion of residues from three conserved enzyme motifs as compared with the apoenzyme, and (iii) an intricate hydrogen-bonding network that includes several water molecules in the active site. Results provide an understanding for the catalytic role of conserved residues in dUTPases.

PubMed: 15208312
DOI: 10.1074/jbc.M406135200

実験手法

X-RAY DIFFRACTION (1.47 Å)