细菌蛋白FimH结构的RMSD分析鉴定了其凝集素结构域的五种构象

Pearl Magala, R. Klevit, W. Thomas, E. Sokurenko, R. Stenkamp
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引用次数: 7

摘要

FimH是一种位于大肠杆菌菌毛顶端的细菌粘附蛋白,其功能是将细菌粘附到宿主细胞上。因此,FimH是细菌感染(如尿路感染)的关键因素,也是药物开发的兴趣所在。它还参与疫苗开发,并作为理解剪切增强捕获键细胞粘附的模型。迄今为止,已经有超过60个结构被储存在蛋白质数据库中,显示了FimH与甘露糖配体、潜在抑制剂和其他毛状蛋白之间的相互作用。除了提供有关配体识别和叶缘组装的见解外,这些结构还提供了对FimH的两个结构域的构象变化的见解,这对其功能至关重要。为了进一步了解这些结构变化,我们在所有这些结构中都添加了FimH的甘露糖结合凝集素结构域,并使用RMSD作为度量将这些结构分为五组凝集素结构域构象。许多结构还包括毛蛋白结构域,它将FimH锚定在毛上,并调节凝集素结构域的构象和功能。对于这些结构,我们还比较了两个畴的相对取向。这些结构分析增强了我们对与FimH配体结合和域-域相互作用相关的构象变化的理解,包括它在细菌粘附中通过变构力作用的捕获键行为。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain
FimH is a bacterial adhesin protein located at the tip of Escherichia coli fimbria that functions to adhere bacteria to host cells. Thus, FimH is a critical factor in bacterial infections such as urinary tract infections and is of interest in drug development. It is also involved in vaccine development and as a model for understanding shear‐enhanced catch bond cell adhesion. To date, over 60 structures have been deposited in the Protein Data Bank showing interactions between FimH and mannose ligands, potential inhibitors, and other fimbrial proteins. In addition to providing insights about ligand recognition and fimbrial assembly, these structures provide insights into conformational changes in the two domains of FimH that are critical for its function. To gain further insights into these structural changes, we have superposed FimH's mannose binding lectin domain in all these structures and categorized the structures into five groups of lectin domain conformers using RMSD as a metric. Many structures also include the pilin domain, which anchors FimH to the fimbriae and regulates the conformation and function of the lectin domain. For these structures, we have also compared the relative orientations of the two domains. These structural analyses enhance our understanding of the conformational changes associated with FimH ligand binding and domain‐domain interactions, including its catch bond behavior through allosteric action of force in bacterial adhesion.
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