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细菌蛋白纳米结构揭示了费里素中的生物矿物化过程

Chacko Jobichen¹, Tan Ying Chong¹, Rajesh Rattinam^1,2

¹Department of Biological Sciences, National University of Singapore, Singapore 117543, Singapore.

|August 2, 2023

概括

这项研究揭示了Streptomyces coelicolor bacterioferritin (ScBfr) 纳米的结构,显示了铁生物矿化阶段. 蛋白质和铁核之间的关键联系解释了铁的储存和贩运机制.

科学领域:

生物化学生物化学
结构生物学结构生物学
微生物学微生物学

背景情况:

费里丁蛋白质形成纳米,对铁代谢至关重要,包括氧化,储存和矿化.
现有的结构缺乏对铁生物矿物质集群和纳米组件的完整视图.
这些纳米内的生物矿物化过程的结构细节通常缺失.

研究的目的:

为了确定Streptomyces coelicolor bacterioferritin (ScBfr) 的apoform和holoforms的冷电子显微镜 (cryo-EM) 结构.
阐明SCBfr纳米内的铁生物矿化和铁贩运的结构基础.

主要方法:

电子显微镜 (cryo-EM) 用于分辨SCBfr的apoform和holoforms的结构.
进行X射线晶体学以确定ScBfr.fr的亚单元晶体结构.
针对位点的突变发生和截断,以研究特定的ScBfr残留物在铁结合中的作用.

主要成果:

在SCBfr纳米中,Holoforms揭示了铁-生物矿物积累的不同阶段.
在特定的纳米道中确定了ScBfr单体的C末端和铁-生物矿物质集群之间的连接.
影响这些连接的突变和切断显著减少了铁和酸盐的结合.

结论:

这些结构为细菌胺纳米提供了原型,详细介绍了铁的生物矿物化.
这些发现揭示了通过纳米内的识别道来贩运铁的机制.
这项工作为细菌中铁的储存和矿化提供了结构性的见解.

关键词:

一个Fe集群.这种菌种是Streptomyces coelicoloror.化-EM结构的结构.类似于费里的分子.纳米子中的纳米子

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