首页> 美国卫生研究院文献>Acta Crystallographica Section F: Structural Biology and Crystallization Communications >Structures of a human blood group glycosyltransferase in complex with a photo-activatable UDP-Gal derivative reveal two different binding conformations
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Structures of a human blood group glycosyltransferase in complex with a photo-activatable UDP-Gal derivative reveal two different binding conformations

机译:与可光活化的UDP-Gal衍生物复合的人类血型糖基转移酶的结构揭示了两个不同的结合构象

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摘要

Glycosyltransferases (GTs) catalyse the sequential addition of monosaccharides to specific acceptor molecules and play major roles in key biological processes. GTs are classified into two main families depending on the inverted or retained stereochemistry of the glycosidic bond formed during the reaction. While the mechanism of inverting enzymes is well characterized, the precise nature of retaining GTs is still a matter of much debate. In an attempt to clarify this issue, studies were initiated to identify reaction-intermediate states by using a crystallographic approach based on caged substrates. In this paper, two distinct structures of AA(Gly)B, a dual-specificity blood group synthase, are described in complex with a UDP-galactose derivative in which the O6′′ atom is protected by a 2-nitrobenzyl group. The distinct conformations of the caged substrate in both structures of the enzyme illustrate the highly dynamic nature of its active site. An attempt was also made to photolyse the caged compound at low temperature, which unfortunately is not possible without damaging the uracil group as well. These results pave the way for kinetic crystallography experiments aiming at trapping and characterizing reaction-intermediate states in the mechanism of enzymatic glycosyl transfer.
机译:糖基转移酶(GTs)催化单糖向特定受体分子的顺序添加,并在关键的生物学过程中起主要作用。根据反应过程中形成的糖苷键的倒置或保留的立体化学,GT分为两个主要家族。尽管转化酶的机制已被很好地表征,但保留GTs的确切性质仍是一个有很多争议的问题。为了澄清这个问题,开始了使用基于笼状底物的晶体学方法来鉴定反应中间状态的研究。在本文中,描述了双特异性血型合酶AA(Gly)B的两个不同结构,该结构与UDP-半乳糖衍生物(其中O6''原子受2-硝基苄基保护)复合。笼罩底物在酶的两种结构中的独特构象说明了其活性位点的高度动态性质。还尝试了在低温下光解笼中的化合物,不幸的是,在不破坏尿嘧啶基团的情况下也是不可能的。这些结果为旨在捕获和表征酶糖基转移机理中反应中间态的动力学晶体学实验铺平了道路。

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