2H1X

Crystal structure of 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein)

2H1X の概要

• エントリーDOI: 10.2210/pdb2h1x/pdb
• 関連するPDBエントリー: 1F41
• 分子名称: 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein) (2 entities in total)
• 機能のキーワード: 5-hydroxyisourate hydrolase, trp, uric acid degradation, allantoin, hydrolase
• 由来する生物種: Danio rerio (zebrafish)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 53040.50

構造登録者

Zanotti, G.,Cendron, L.,Folli, C.,Ramazzina, I.,Percudani, R.,Berni, R. (登録日: 2006-05-17, 公開日: 2006-10-31, 最終更新日: 2023-08-30)

主引用文献

Zanotti, G.,Cendron, L.,Ramazzina, I.,Folli, C.,Percudani, R.,Berni, R.
Structure of Zebra fish HIUase: Insights into Evolution of an Enzyme to a Hormone Transporter.
J.Mol.Biol., 363:1-9, 2006

PubMed Abstract: During early vertebrate evolution, a duplication event in the gene encoding 5-hydroxyisourate hydrolase (HIUase), a widely distributed enzyme of purine metabolism, gave rise to transthyretin (TTR), a thyroid hormone transporter. We report here on the crystal structure of zebra fish HIUase in two different crystal forms. Despite the phylogenetic distance, this structure compares well with those of newly characterized bacterial HIUases, especially with regard to catalytic regions, which are highly preserved. Comparison with TTR structure reveals a highly conserved scaffold, harbouring distinct functional sites located in the same regions of the two vertebrate proteins. Residues that are differentially conserved in HIUases compared to TTR map in putative catalytic regions occupying significant portions of the two halves of a central channel that transverses the whole TTR protein. The evolution of TTR has been accompanied by remarkable changes of the HIUase active sites that gave rise to a channel open at both ends, thus allowing free access to hormone molecules.

PubMed: 16952372
DOI: 10.1016/j.jmb.2006.07.079

実験手法

X-RAY DIFFRACTION (1.98 Å)