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发现FPM13的发现和冷EM结构,FPM13是一种Periplasmic金属蛋白,是弗朗西塞拉独特的
Daniel L Clemens1, Bai-Yu Lee1, Xiaoyu Liu2,3
1Department of Medicine, UCLA, Los Angeles, CA 90095, USA.
bioRxiv : the preprint server for biology
|July 14, 2025
概括
我们发现了一种新的蛋白质,FPM13,它是弗朗西塞拉细菌特有的. 这种13kDa的周等离子金属蛋白形成了一个甜甜圈形状的结构,可能在金属运输或排毒中发挥作用.
科学领域:
- 微生物学 微生物学
- 结构生物学 结构生物学
- 生物化学 生物化学
背景情况:
- 来自弗朗西塞拉属的FTN_1118蛋白最初是在6型分泌系统 (T6SS) 功效器的净化过程中鉴定出来的.
- 它的功能和结构以前是未知的,需要详细的调查.
研究的目的:
- 确定新型弗朗西塞拉蛋白FTN_1118.18的结构和生物化学特性.
- 为了阐明其细胞本地化及其在弗朗西塞拉属内的潜在生物功能.
主要方法:
- 使用冷电子显微镜 (cryoEM) 和cryoID方法进行结构性确定.
- 使用了包括APEX-生物化和Triton X-114相分割在内的生物化学测定.
- 诱导合等离子体质谱法 (ICP-MS) 用于评估金属结合.
主要成果:
- FTN_1118的结构被指定为FPM13 (弗朗西塞拉周等离子体金属蛋白,13kDa),被确定为一个独特的13kDa周等离子体蛋白.
- FPM13形成了一个对称的,甜甜圈形状的18-mer复合体,其中有一个中心通道,具有β-sheet核心和α-helical shell.
- 生物化学分析证实FPM13是一种可溶性周等离子蛋白,可以结合铁和铜.
结论:
- FPM13是一种新的,属性特定的Francisella蛋白质,具有独特的18-mer甜甜圈形结构.
- FPM13是一种环等离子金属蛋白,能结合铁和铜.
- 虽然FPM13的删除没有影响细菌的生长,但在缺乏铁的条件下,它导致铜的敏感性增加,这表明它在金属稳态或解毒中发挥了作用.
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