2h1x: Difference between revisions

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==Overview==

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.

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 Structure==

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[[Category: uric acid degradation]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:23 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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 Structure==
@@ Line 25: / Line 25: @@
 [[Category: uric acid degradation]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 20:12:48 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:37:23 2008''