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2Q37

Crystal structure of OHCU decarboxylase in the presence of (S)-allantoin

2Q37 の概要
エントリーDOI10.2210/pdb2q37/pdb
分子名称OHCU decarboxylase, 1-[(4S)-2,5-DIOXOIMIDAZOLIDIN-4-YL]UREA (3 entities in total)
機能のキーワードohcu, 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline, plant protein, lyase
由来する生物種Arabidopsis thaliana (thale cress)
細胞内の位置Cell membrane; Peripheral membrane protein: Q9LVM5
タンパク質・核酸の鎖数1
化学式量合計20995.28
構造登録者
Kim, K. (登録日: 2007-05-30, 公開日: 2007-06-12, 最終更新日: 2024-10-30)
主引用文献Kim, K.,Park, J.,Rhee, S.
Structural and functional basis for (s)-allantoin formation in the ureide pathway.
J.Biol.Chem., 282:23457-23464, 2007
Cited by
PubMed Abstract: The ureide pathway, which mediates the oxidative degradation of uric acid to (S)-allantoin, represents the late stage of purine catabolism in most organisms. The details of uric acid metabolism remained elusive until the complete pathway involving three enzymes was recently identified and characterized. However, the molecular details of the exclusive production of one enantiomer of allantoin in this pathway are still undefined. Here we report the crystal structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU) decarboxylase, which catalyzes the last reaction of the pathway, in a complex with the product, (S)-allantoin, at 2.5-A resolution. The homodimeric helical protein represents a novel structural motif and reveals that the active site in each monomer contains no cofactors, distinguishing this enzyme mechanistically from other cofactor-dependent decarboxylases. On the basis of structural analysis, along with site-directed mutagenesis, a mechanism for the enzyme is proposed in which a decarboxylation reaction occurs directly, and the invariant histidine residue in the OHCU decarboxylase family plays an essential role in producing (S)-allantoin through a proton transfer from the hydroxyl group at C4 to C5 at the re-face of OHCU. These results provide molecular details that address a longstanding question of how living organisms selectively produce (S)-allantoin.
PubMed: 17567580
DOI: 10.1074/jbc.M703211200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 2q37
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-11に公開中

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