Near-atomic cryo-EM structure of the light-harvesting complex LH2 from the sulfur purple bacterium Ectothiorhodospira haloalkaliphila

IF 4.4 2区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Structure Pub Date : 2024-12-17 DOI:10.1016/j.str.2024.11.015
Anna D. Burtseva, Timur N. Baymukhametov, Maxim A. Bolshakov, Zoya К. Makhneva, Andrey V. Mardanov, Andrey M. Tsedilin, Huawei Zhang, Vladimir.O. Popov, Aleksandr A. Ashikhmin, Konstantin M. Boyko
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Abstract

Bacteria with the simplest system for solar energy absorption and conversion use various types of light-harvesting complexes for these purposes. Light-harvesting complex 2 (LH2), an important component of the bacterial photosynthetic apparatus, has been structurally well characterized among purple non-sulfur bacteria. In contrast, so far only one high-resolution LH2 structure from sulfur bacteria is known. Here, we report the near-atomic resolution cryoelectron microscopy (cryo-EM) structure of the LH2 complex from the purple sulfur bacterium Ectothiorhodospira haloalkaliphila, which allowed us to determine the predominant polypeptide composition of this complex and the identification of the most probable type of its carotenoid. Comparison of our structure with the only known LH2 complex from a sulfur bacterium revealed severe differences in the overall ring-like organization. Expanding the architectural universe of bacterial light-harvesting complexes, our results demonstrate that, as observed for non-sulfur bacteria, the LH2 complexes of sulfur bacteria may also exhibit various types of spatial organization.

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紫色硫杆菌中的采光复合物 LH2 的近原子低温电子显微镜结构
细菌具有最简单的太阳能吸收和转换系统,利用各种类型的光收集复合体来实现这些目的。光收集复合体 2(LH2)是细菌光合作用装置的重要组成部分,其结构特征在紫色非硫细菌中已得到很好的描述。相比之下,迄今为止人们只知道硫细菌的一种高分辨率 LH2 结构。在此,我们报告了来自紫色硫细菌 Ectothiorhodospira haloalkaliphila 的 LH2 复合物的近原子分辨率冷冻电子显微镜(cryo-EM)结构,从而确定了该复合物的主要多肽组成,并鉴定了其类胡萝卜素的最可能类型。将我们的结构与唯一已知的来自硫细菌的 LH2 复合物进行比较后发现,两者在整体环状组织结构上存在严重差异。我们的研究结果拓展了细菌采光复合物的结构领域,证明正如在非硫细菌中观察到的那样,硫细菌的 LH2 复合物也可能表现出各种类型的空间组织。
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来源期刊
Structure
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.
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