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首页> 外文期刊>Journal of Molecular Biology >Structure of Zebra fish HIUase: Insights into Evolution of an Enzyme to a Hormone Transporter.
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Structure of Zebra fish HIUase: Insights into Evolution of an Enzyme to a Hormone Transporter.

机译：斑马鱼HIUase的结构：洞悉酶向激素转运蛋白的进化。

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摘要

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.
机译：在早期脊椎动物进化过程中，编码5-羟基异羟乙酸水解酶（HIUase）（嘌呤代谢的一种广泛分布的酶）的基因发生重复事件，产生了甲状腺激素转运蛋白转甲状腺素蛋白（TTR）。我们在这里报告了斑马鱼HIUase的两种不同晶体形式的晶体结构。尽管有系统发育距离，但该结构与新鉴定的细菌HIUase的结构相当，特别是在高度保留的催化区域方面。与TTR结构的比较揭示了高度保守的支架，在两个脊椎动物蛋白的相同区域中具有不同的功能位点。与TTR图相比，HIUase中在TIU图中差异保守的残基占据了横跨整个TTR蛋白的中央通道的两半的重要部分。 TTR的进化伴随着HIUase活性位点的显着变化，从而在两端形成了开放的通道，从而使激素分子可以自由进入。

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