3E74

Crystal structure of E. coli allantoinase with iron ions at the metal center

3E74 の概要

• エントリーDOI: 10.2210/pdb3e74/pdb
• 関連するPDBエントリー: 3E75
• 分子名称: Allantoinase, FE (III) ION (3 entities in total)
• 機能のキーワード: (beta/alpha)8-barrel domain, small beta-sheet domain, hydrolase, metal-binding, purine metabolism, zinc
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 210856.85

構造登録者

Kim, K. (登録日: 2008-08-17, 公開日: 2009-02-24, 最終更新日: 2021-11-10)

主引用文献

Kim, K.,Kim, M.I.,Chung, J.,Ahn, J.H.,Rhee, S.
Crystal structure of metal-dependent allantoinase from Escherichia coli
J.Mol.Biol., 387:1067-1074, 2009

PubMed Abstract: Allantoinase acts as a key enzyme for the biogenesis and degradation of ureides by catalyzing the conversion of (S)-allantoin into allantoate, the final step in the ureide pathway. Despite limited sequence similarity, biochemical studies of the enzyme suggested that allantoinase belongs to the amidohydrolase family. In this study, the crystal structure of allantoinase from Escherichia coli was determined at 2.1 A resolution. The enzyme consists of a homotetramer in which each monomer contains two domains: a pseudo-triosephosphate-isomerase barrel and a beta-sheet. Analogous to other enzymes in the amidohydrolase family, allantoinase retains a binuclear metal center in the active site, embedded within the barrel fold. Structural analyses demonstrated that the metal ions in the active site ligate one hydroxide and six residues that are conserved among allantoinases from other organisms. Functional analyses showed that the presence of zinc in the metal center is essential for catalysis and enantioselectivity of substrate. Both the metal center and active site residues Asn94 and Ser317 play crucial roles in dictating enzyme activity. These structural and functional features are distinctively different from those of the metal-independent allantoinase, which was very recently identified.

PubMed: 19248789
DOI: 10.1016/j.jmb.2009.02.041

実験手法

X-RAY DIFFRACTION (2.1 Å)