Structural insights into polyisoprenyl-binding glycosyltransferases

IF 4.3 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Structure Pub Date : 2025-01-29 DOI:10.1016/j.str.2025.01.003

Allen P. Zinkle, Ryan T. Morgan, Rie Nygaard, Filippo Mancia

引用次数: 0

Abstract

Glycosyltransferases (GTs) catalyze the addition of sugars to diverse substrates facilitating complex glycoconjugate biosynthesis across all domains of life. When embedded in or associated with the membrane, these enzymes often depend on polyisoprenyl-phosphate or -pyrophosphate (PP) lipid carriers, including undecaprenyl phosphate in bacteria and dolichol phosphate in eukaryotes, to transfer glycan moieties. GTs that bind PP substrates (PP-GTs) are functionally diverse but share some common structural features within their family or subfamily, particularly with respect to how they interact with their cognate PP ligands. Recent advances in single-particle cryo-electron microscopy (cryo-EM) have provided insight into the structures of PP-GTs and the modes by which they bind their PP ligands. Here, we explore the structural landscape of PP-GTs, focusing mainly on those for which there is molecular-level information on liganded states, and highlight how PP coordination modalities may be shared or differ among members of this diverse enzyme class.

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聚异戊二基结合糖基转移酶的结构分析

糖基转移酶（GTs）催化糖添加到不同的底物，促进复杂的糖缀合生物合成在所有生命领域。当嵌入或与膜结合时，这些酶通常依赖于聚异戊烯基磷酸或焦磷酸（PP）脂质载体，包括细菌中的十一戊烯基磷酸和真核生物中的磷酸二醇，来转移聚糖部分。结合PP底物的GTs （PP-GTs）功能多样，但在其家族或亚家族中具有一些共同的结构特征，特别是它们如何与同源PP配体相互作用。单粒子低温电子显微镜（cryo-EM）的最新进展为PP- gt的结构和它们结合PP配体的模式提供了深入的了解。在这里，我们探索了PP- gt的结构景观，主要关注那些具有配体状态分子水平信息的结构，并强调了PP配位方式在这一不同酶类成员之间是如何共享或不同的。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

期刊介绍： Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome. In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.