Structure of the Nucleotide-Diphospho-Sugar Transferase, SpsA from Bacillus subtilis, in Native and Nucleotide-Complexed Forms

详细信息    查看全文

• 作者：Simon J. Charnock and Gideon J. Davies
• 刊名：Biochemistry
• 出版年：1999
• 出版时间：May 18, 1999
• 年：1999
• 卷：38
• 期：20
• 页码：6380 - 6385
• 全文大小：116K
• 年卷期：v.38,no.20(May 18, 1999)
• ISSN：1520-4995

文摘

The enzymatic formation of glycosidic bonds may be catalyzed by the transfer of the glycosylmoiety 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 includecellulose synthase and many lipopolysaccharide and bacterial O-antigen synthases. The three-dimensionalcrystal structure of SpsA has been determined by conventional MIR techniques at a resolution of 1.5 Å.It is a two-domain protein with a nucleotide-binding domain together with an acceptor binding domainwhich features a disordered loop spanning the active site. The structures of SpsA in complex with bothMg-UDP and Mn-UDP have also been determined at 2.0 and 1.7 Å, respectively. These complexes,together with the sequence conservation, begin to shed light on the mechanism of this ubiquitous familyof inverting glycosyltransferases.