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首页> 外文期刊>Biochemistry >Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms.
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Structure of the nucleotide-diphospho-sugar transferase, SpsA from Bacillus subtilis, in native and nucleotide-complexed forms.

机译：枯草芽孢杆菌的核苷酸二磷酸糖转移酶SpsA的结构为天然形式和核苷酸复合形式。

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摘要

The enzymatic formation of glycosidic bonds may be catalyzed by the transfer of the glycosyl moiety from an activated nucleotide-diphospho-sugar donor to a specific acceptor. SpsA is a glycosyltransferase implicated in the synthesis of the spore coat of Bacillus subtilis, whose homologues include cellulose synthase and many lipopolysaccharide and bacterial O-antigen synthases. The three-dimensional crystal structure of SpsA has been determined by conventional MIR techniques at a resolution of 1.5 A. It is a two-domain protein with a nucleotide-binding domain together with an acceptor binding domain which features a disordered loop spanning the active site. The structures of SpsA in complex with both Mg-UDP and Mn-UDP have also been determined at 2.0 and 1.7 A, respectively. These complexes, together with the sequence conservation, begin to shed light on the mechanism of this ubiquitous family of inverting glycosyltransferases.
机译：糖苷键的酶促形成可以通过糖基部分从活化的核苷酸-二磷酸-糖供体向特定受体的转移来催化。 SpsA是一种糖基转移酶，参与枯草芽孢杆菌的孢子外皮的合成，其同源物包括纤维素合酶和许多脂多糖和细菌O抗原合酶。 SpsA的三维晶体结构已通过常规MIR技术在1.5 A的分辨率下确定。它是一个具有核苷酸结合结构域和受体结合结构域的两域蛋白，其特征是跨越活性位点的无序环。与Mg-UDP和Mn-UDP配合使用的SpsA的结构也分别在2.0和1.7 A下确定。这些复合物与序列保守性一起开始阐明这种普遍存在的倒置糖基转移酶家族的机制。

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