2h1x
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Crystal structure of 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein)
OverviewOverview
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.
About this StructureAbout this Structure
2H1X is a Single protein structure of sequence from Danio rerio. Active as Hydroxyisourate hydrolase, with EC number 3.5.2.17 Full crystallographic information is available from OCA.
ReferenceReference
Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter., Zanotti G, Cendron L, Ramazzina I, Folli C, Percudani R, Berni R, J Mol Biol. 2006 Oct 13;363(1):1-9. Epub 2006 Aug 2. PMID:16952372
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