Information Materials and Intelligent Sensing Laboratory of Anhui Province, Institutes of Material Science and Information Technology, Anhui University, Hefei 230601, China.
School of Resources and Environmental Engineering, Anhui University, Hefei 230601, China.
Int J Mol Sci. 2023 Oct 23;24(20):15491. doi: 10.3390/ijms242015491.
N-acetyl sugar amidotransferase (NASAT) is involved in the lipopolysaccharide (LPS) biosynthesis pathway that catalyzes the formation of the acetamido moiety (sugar-NC(=NH)CH3) on the O-chain. So far, little is known about its structural and functional properties. Here, we report the crystal structure of an N-acetyl sugar amidotransferase from (LpNASAT) at 2.33 Å resolution. LpNASAT folds into a compact basin-shaped architecture with an unusually wide and open putative substrate-binding pocket and a conserved zinc ion-binding tetracysteine motif. The pocket contains a Rossmann-like fold with a PP-loop, suggesting that the NASAT-catalyzed amidotransfer reaction probably requires the conversion of ATP to AMP and PPi. Our data provide structural insights into the NASAT family of proteins, and allow us to possibly identify its functionally important regions.
N-乙酰氨基糖基转移酶（NASAT）参与脂多糖（LPS）生物合成途径，该途径催化 O-链上乙酰氨基部分（糖-NC(=NH)CH3）的形成。到目前为止，人们对其结构和功能特性知之甚少。在这里，我们报告了来自 （LpNASAT）的 N-乙酰氨基糖基转移酶的晶体结构，分辨率为 2.33 Å。LpNASAT 折叠成一个紧凑的盆状结构，具有异常宽且开放的假定底物结合口袋和保守的锌离子结合四半胱氨酸基序。口袋包含一个具有 PP 环的 Rossmann 样折叠，表明 NASAT 催化的转酰胺反应可能需要将 ATP 转化为 AMP 和 PPi。我们的数据为 NASAT 家族蛋白提供了结构见解，并使我们有可能确定其功能重要区域。
