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首页> 外文期刊>Biochemistry >Structural Studies of the Spinosyn Forosaminyltransferase, SpnP
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Structural Studies of the Spinosyn Forosaminyltransferase, SpnP

机译：Spinosyn异丁香转移酶SpnP的结构研究

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摘要

Spinosyns A and D (spinosad) are complex polyketide natural products biosynthesized through the cooperation of a modular polyketide synthase and several tailoring enzymes. SpnP catalyzes the final tailoring step, transferring forosamine from a TDP-D-forosamine donor substrate to a spinosyn pseudoaglycone acceptor substrate. Sequence analysis indicated that SpnP belongs to a small group of glycosyltransferases (GTs) that require an auxiliary protein for activation. However, unlike other GTs in this subgroup, no putative auxiliary protein gene could be located in the biosynthetic gene cluster. To learn more about SpnP, the structures of SpnP and its complex with TDP were determined to 2.50 and 3.15 ? resolution, respectively. Binding of TDP causes the reordering of several residues in the donor substrate pocket. SpnP possesses a structural feature that has only been previously observed in the related glycosyltransferase EryCIII, in which it mediates association with the auxiliary protein EryCII. This motif, H-X-R-X_5-D-X_5-R-X_(12?20)-D-P-X_3-W-L-X_(12?18)-E-X_4-G, may be predictive of glycosyltransferases that interact with an auxiliary protein. A reverse glycosyl transfer assay demonstrated that SpnP possesses measurable activity in the absence of an auxiliary protein. Our data suggest that SpnP can bind its donor substrate by itself but that the glycosyl transfer reaction is facilitated by an auxiliary protein that aids in the correct folding of a flexible loop surrounding the pseudoaglycone acceptor substrate-binding pocket.
机译：Spinosyns A和D（spinosad）是复杂的聚酮化合物天然产物，是通过模块化聚酮化合物合酶和几种定制酶的协同作用而生物合成的。 SpnP催化最后的剪裁步骤，将甲胺从TDP-D-甲胺供体转移至多杀菌素假糖苷配体受体。序列分析表明，SpnP属于糖基转移酶（GTs）的一小部分，需要辅助蛋白才能激活。但是，与该亚组中的其他GT不同，在生物合成基因簇中没有推定的辅助蛋白基因。为了进一步了解SpnP，将SpnP及其与TDP的复合物的结构确定为2.50和3.15？分辨率分别。 TDP的结合导致供体底物袋中几个残基的重新排序。 SpnP具有以前仅在相关的糖基转移酶EryCIII中介导的结构特征，其中它与辅助蛋白EryCII介导缔合。该基序HXR-X_5-D-X_5-R-X_（12？20）-DP-X_3-WL-X_（12？18）-E-X_4-G可以预测与辅助蛋白相互作用的糖基转移酶。反向糖基转移分析表明，在没有辅助蛋白的情况下，SnP具有可测量的活性。我们的数据表明，SnP可以自身结合其供体底物，但糖基转移反应是由辅助蛋白促进的，该辅助蛋白有助于围绕假糖苷配体受体底物结合口袋的柔性环的正确折叠。

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