Asymmetric structure of podophage N4 from the Schitoviridae family reveals a type of tube-sheath short-tail architecture

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY

Structure Pub Date : 2025-05-02 DOI:10.1016/j.str.2025.04.008

Jing Zheng, Hao Pang, Hao Xiao, Junquan Zhou, Zhonghua Liu, Wenyuan Chen, Hongrong Liu

引用次数: 0

Abstract

The tails of the majority of reported podophages are typically composed of an adaptor, a nozzle, and a needle, and flanked by six or twelve fibers. However, the Schitoviridae family, as represented by podophage N4, exhibits a different tail architecture that remains poorly understood. In this study, we employed cryoelectron microscopy (cryo-EM) to determine the atomic structures of mature and empty podophage N4 particles. The N4 tail, which is connected to the head by a portal and flanked by 12 fibers, comprises an adaptor, a 12-fold extended tail tube encircled by a 6-fold tail sheath, and a plug. The extended tail sheath is composed of two proteins, gp65 and gp64. Furthermore, we identified two distinct tail conformations in the mature podophage N4. Our structures provide insights into the mechanisms of ejection and early transcription of podophage N4, as well as for N4-like phages and CrAssphages.

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Schitoviridae家族的足噬体N4的不对称结构揭示了一种管鞘短尾结构

大多数报道的足噬体的尾部通常由一个接头、一个喷嘴和一个针组成，两侧有6或12根纤维。然而，以podophage N4为代表的Schitoviridae家族表现出一种不同的尾部结构，这一点仍然知之甚少。在这项研究中，我们使用冷冻电镜（cryo-EM）来确定成熟和空的podophage N4颗粒的原子结构。N4尾部通过入口连接到头部，两侧有12根纤维，包括适配器、由6倍尾护套环绕的12倍延长尾管和插头。延长的尾鞘由gp65和gp64两种蛋白组成。此外，我们在成熟的podophage N4中发现了两种不同的尾部构象。我们的结构提供了对podophage N4，以及N4样噬菌体和crassphage的喷射和早期转录机制的见解。

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.