2H1X
Crystal structure of 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein)
Summary for 2H1X
| Entry DOI | 10.2210/pdb2h1x/pdb |
| Related | 1F41 |
| Descriptor | 5-hydroxyisourate Hydrolase (formerly known as TRP, Transthyretin Related Protein) (2 entities in total) |
| Functional Keywords | 5-hydroxyisourate hydrolase, trp, uric acid degradation, allantoin, hydrolase |
| Biological source | Danio rerio (zebrafish) |
| Total number of polymer chains | 4 |
| Total formula weight | 53040.50 |
| Authors | Zanotti, G.,Cendron, L.,Folli, C.,Ramazzina, I.,Percudani, R.,Berni, R. (deposition date: 2006-05-17, release date: 2006-10-31, Last modification date: 2023-08-30) |
| Primary citation | 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 Cited by 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: 16952372DOI: 10.1016/j.jmb.2006.07.079 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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