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首页> 外文期刊>Journal of Molecular Biology >Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases.
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Three-dimensional structures of the Mn and Mg dTDP complexes of the family GT-2 glycosyltransferase SpsA: a comparison with related NDP-sugar glycosyltransferases.

机译：GT-2糖基转移酶SpsA家族的Mn和Mg dTDP复合物的三维结构：与相关NDP-糖基糖基转移酶的比较。

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摘要

The vast majority of glycosidic-bond synthesis in nature is performed by glycosyltransferases, which use activated glycosides as the sugar donor. Typically, the activated leaving group is a nucleoside phosphate, lipid phosphate or phosphate. The nucleotide-sugar-dependent glycosyltransferases fall into over 50 sequence-based families, with the largest and most widespread family of inverting transferases named family GT-2. Here, we present the three-dimensional crystal structure of SpsA, the first and currently the only structural representative from family GT-2, in complex with both Mn-dTDP and Mg-dTDP at a resolution of 2 A. These structures reveal how SpsA and related enzymes may display nucleotide plasticity and permit a comparison of the catalytic centre of this enzyme with those from related sequence families whose three-dimensional structures have recently been determined. Family GT-2 enzymes, together with enzymes from families 7, 13 and 43, appear to form a clan of related structures with identical catalytic apparatus and reaction mechanism. Copyright 2001 Academic Press.
机译：自然界中绝大多数的糖苷键合成是由糖基转移酶完成的，后者使用活化的糖苷作为糖供体。通常，活化的离去基团是核苷磷酸酯，脂质磷酸酯或磷酸酯。核苷酸糖依赖性糖基转移酶属于超过50个基于序列的家族，其中最大和最广泛的转化转移酶家族称为GT-2家族。在这里，我们介绍SpsA的三维晶体结构，它是GT-2家族的第一个也是目前唯一的结构代表，与Mn-dTDP和Mg-dTDP都以2 A的分辨率复合。这些结构揭示了SpsA如何并且相关的酶可以显示核苷酸可塑性，并且可以将该酶的催化中心与最近确定了三维结构的相关序列家族的催化中心进行比较。 GT-2家族的酶与家族7、13和43的酶一起似乎形成了具有相同催化装置和反应机理的相关结构族。版权所有2001学术出版社。

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