PUBLICATION
Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter
- Authors
- Zanotti, G., Cendron, L., Ramazzina, I., Folli, C., Percudani, R., and Berni, R.
- ID
- ZDB-PUB-061222-13
- Date
- 2006
- Source
- Journal of molecular biology 363(1): 1-9 (Journal)
- Registered Authors
- Keywords
- 5-hydroxyisourate hydrolase, transthyretin, molecular evolution, uric acid degradation, thyroid hormones
- MeSH Terms
-
- Phylogeny
- Receptors, Albumin/chemistry
- Receptors, Albumin/metabolism
- Amino Acid Sequence
- Animals
- Amidohydrolases/chemistry*
- Amidohydrolases/metabolism
- Evolution, Molecular*
- Thyroid Hormones/metabolism*
- Biological Transport, Active
- Crystallography, X-Ray
- Humans
- Zebrafish*
- Molecular Sequence Data
- Protein Binding
- Zebrafish Proteins/chemistry*
- Zebrafish Proteins/metabolism
- Prealbumin/metabolism*
- PubMed
- 16952372 Full text @ J. Mol. Biol.
Citation
Zanotti, G., Cendron, L., Ramazzina, I., Folli, C., Percudani, R., and Berni, R. (2006) Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter. Journal of molecular biology. 363(1):1-9.
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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping