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首页> 外文期刊>Biochemistry >Structure and Mechanism of the Siderophore-Interacting Protein from the Fuscachelin Gene Cluster of Thermobifida fusca
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Structure and Mechanism of the Siderophore-Interacting Protein from the Fuscachelin Gene Cluster of Thermobifida fusca

机译：嗜热双歧杆菌Fuscachelin基因簇中铁载体相互作用蛋白的结构与机理

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摘要

Microbial iron acquisition is a complex process and frequently a key and necessary step for survival. Among the several paths for iron assimilation, small molecule siderophore-mediated transport is a commonly employed strategy of many microorganisms. The chemistry and biology of the extraordinary tight and specific binding of siderophores to metal is also exploited in therapeutic treatments for microbial virulence and metal toxicity. The intracellular fate of iron acquired via the siderophore pathway is one of the least understood steps in the complex process at the molecular level. A common route to cellular incorporation is the single-electron reduction of ferric to ferrous iron catalyzed by specific and/or nonspecific reducing agents. The biosynthetic gene clusters for siderophores often contain representatives of one or two families of redox-active enzymes: the flavin-containing "siderophore-interacting protein" and iron sulfur ferric siderophore reductases. Here we present the structure and characterization of the siderophore-interacting protein, FscN, from the fuscachelin siderophore gene cluster of Thermobifida fusca. The structure shows a flavoreductase fold with a noncovalently bound FAD cofactor along with an unexpected metal bound adjacent to the flavin site. We demonstrated that FscN is redox-active and measured the binding and reduction of ferric fuscachelin. This work provides a structural basis for the activity of a siderophore-interacting protein and further insight into the complex and important process of iron acquisition and utilization.
机译：微生物铁的获取是一个复杂的过程，通常是生存的关键和必要步骤。在铁同化的几种途径中，小分子铁载体介导的运输是许多微生物的常用策略。铁载体与金属的异常紧密和特异结合的化学和生物学也被用于微生物毒力和金属毒性的治疗中。通过铁载体途径获得的铁的细胞内命运是在分子水平上复杂过程中最少被理解的步骤之一。细胞掺入的常见途径是通过特异性和/或非特异性还原剂将铁单电子还原成亚铁。铁载体的生物合成基因簇通常包含一或两个氧化还原活性酶家族的代表：含黄素的“铁载体相互作用蛋白”和铁硫铁铁载体还原酶。在这里，我们介绍了来自Thermobifida fusca的富斯卡林铁载体基因簇的铁载体相互作用蛋白FscN的结构和特征。该结构显示出带有非共价结合的FAD辅因子的flavoureductase折叠，以及与黄素位点相邻的意外金属结合。我们证明了FscN具有氧化还原活性，并测量了铁补沙蛋白的结合和还原。这项工作为铁载体相互作用蛋白的活性提供了结构基础，并进一步了解了铁的获取和利用的复杂而重要的过程。

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