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首页> 外文期刊>Biochemistry >Conservation and Covariance in Small Bacterial Phosphoglycosyltransferases Identify the Functional Catalytic Core
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Conservation and Covariance in Small Bacterial Phosphoglycosyltransferases Identify the Functional Catalytic Core

机译：小细菌磷酸糖基转移酶的保守性和协方差确定功能性催化核心

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摘要

Phosphoglycosyltransferases (PGTs) catalyze the transfer of a C1' - phosphosugar from a soluble sugar nucleotide diphosphate to a polyprenol phosphate. These enzymes act at the membrane interface, forming the first membrane-associated intermediates in the biosynthesis of cell-surface glycans and glycoconjugates,, including glycoproteins, glycolipids, and the peptidoglycan an bacteria PGTs vary greatly in both their membrane topologies and their substrate preferences. PGTs, such as MraY and WecA are polytopic while other families of,uniquely prokaryotic enzymes have only a single predicted transmembrane helix. PgIC, a PGT involved in the biosynthesis of N-linked glycoproteins in the enteropathogen Campylobacter jejuni is representative of one of the structurally most simple members of the diverse family of small bacterial PGT enzymes. Herein, we apply bioinfomatics and covariance-weighted distance constraints in geometry- and homology-based model building, together with mutational analysis, to investigate monotopic PGTs. The pool of 15000 sequences that are analyzed include the PglC-like enzymes, AS well as sequences from two other related PGTs that contain a "PglC-like" domain embedded-in their larger structures (namely, the bifunctional PglB family; typified by PglB from Neisseria gonorrheae, and WbaP-like enzymes, typified by WbaP from Salmonella enterica):Including these two subfamilies of PGTs in the analysis highlights key residues conserved across, all three families, of small bacterial PGTS. Mutagenesis analysis of these conserved residues provides further information about the::: essentiality of many of these residues in catalysis. Construction of a structural model of the cytosolic globular domain utilizing Three-dimensional distance constraints, provided by conservation covariance analysis, provides additional insight-into the catalytic Core of these families of small bacterial PGT enzymes.
机译：磷酸糖基转移酶（PGTs）催化将C1'-磷酸糖从可溶性糖核苷酸二磷酸酯转移至聚戊二烯磷酸酯。这些酶作用于膜界面，在细胞表面聚糖和糖结合物（包括糖蛋白，糖脂和肽聚糖）的生物合成中形成了第一个与膜相关的中间体，细菌PGT的膜拓扑结构和底物偏好差异很大。 PGT，例如MraY和WecA是多位的，而其他的原核生物酶家族只有一个预测的跨膜螺旋。 PgIC，参与空肠弯曲杆菌空肠弯曲杆菌N连接糖蛋白生物合成的PGT，是小细菌PGT酶多样化家族中结构最简单的成员之一。在这里，我们在基于几何和同源性的模型构建中应用生物信息学和协方差加权距离约束，并进行突变分析，以研究单位PGT。分析的15000个序列库包括PglC样酶，AS以及来自其他两个相关PGT的序列，这些序列在其较大结构中嵌入了“ PglC样”结构域（即双功能PglB家族;以PglB为代表） （来自淋病奈瑟氏球菌）和WbaP样酶，以小肠沙门氏菌（Salmonella enterica）为代表）：将PGT的这两个亚家族包括在分析中，可突出显示这三个家族中小细菌PGTS保守的关键残基。这些保守残基的诱变分析提供了有关以下方面的更多信息：催化许多这些残基。利用保守性协方差分析提供的利用三维距离约束的胞质球状结构域结构模型的构建，为这些小细菌PGT酶家族的催化核心提供了更多的见识。

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