Cryo-EM structure of the SPFH-NfeD family protein complex QmcA-YbbJ

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Structure Pub Date : 2024-08-23 DOI:10.1016/j.str.2024.07.022

Kwan Ann Tan, Zhu Qiao, Zachary Ze En Lim, Joshua Yi Yeo, Yonlada Yong, Phong Hoa Do, Ero Rya, Yong-Gui Gao

引用次数: 0

Abstract

The SPFH (stomatin, prohibitin, flotillin, and HflK/C) protein family is universally present and encompasses the evolutionarily conserved SPFH domain. These proteins are predominantly localized in lipid raft and implicated in various biological processes. The NfeD (nodulation formation efficiency D) protein family is often encoded in tandem with SPFH proteins, suggesting a close functional relationship. Here, we elucidate the cryoelectron microscopy (cryo-EM) structure of the Escherichia coli QmcA-YbbJ complex belonging to the SPFH and NfeD families, respectively. Our findings reveal that the QmcA-YbbJ complex forms an intricate cage-like structure composed of 26 copies of QmcA-YbbJ heterodimers. The transmembrane helices of YbbJ act as adhesive elements bridging adjacent QmcA molecules, while the oligosaccharide-binding domain of YbbJ encapsulates the SPFH domain of QmcA. Our structural study significantly contributes to understanding the functional role of the NfeD protein family and sheds light on the interplay between SPFH and NfeD family proteins.

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SPFH-NfeD 家族蛋白复合物 QmcA-YbbJ 的冷冻电镜结构

SPFH（stomatin、phibitin、flotillin 和 HflK/C）蛋白家族普遍存在，包含进化保守的 SPFH 结构域。这些蛋白主要定位于脂质筏，与各种生物过程有关。NfeD（结核形成效率 D）蛋白家族通常与 SPFH 蛋白串联编码，这表明它们之间存在密切的功能关系。本文阐明了分别属于 SPFH 和 NfeD 家族的大肠杆菌 QmcA-YbbJ 复合物的冷冻电子显微镜（cryo-EM）结构。我们的研究结果表明，QmcA-YbbJ复合体形成了一个复杂的笼状结构，由26个拷贝的QmcA-YbbJ异源二聚体组成。YbbJ 的跨膜螺旋作为粘合元件连接相邻的 QmcA 分子，而 YbbJ 的寡糖结合结构域则包裹着 QmcA 的 SPFH 结构域。我们的结构研究大大有助于理解 NfeD 蛋白家族的功能作用，并揭示了 SPFH 和 NfeD 家族蛋白之间的相互作用。

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.