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首页> 外文期刊>Metallomics. integrated biometal science >Flexible aspartates propel iron to the ferroxidation sites along pathways stabilized by a conserved arginine in Dps proteins from Mycobacterium smegmatis
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Flexible aspartates propel iron to the ferroxidation sites along pathways stabilized by a conserved arginine in Dps proteins from Mycobacterium smegmatis

机译：柔性天冬氨酸沿着来自分枝杆菌的DPS蛋白质中的保守精氨酸稳定的途径将熨斗延伸到铁氧化位点

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摘要

DNA-binding proteins under starvation (Dps) are dodecameric nano-compartments for iron oxidation and storage in bacterial cells. These proteins have roughly spherical structures with a hollow interior where iron is stored. Through mutational analysis of a conserved arginine residue in the second Dps protein from Mycobacterium smegmatis, we have identified residues which stabilize the interfaces between the iron entry and ferroxidation sites. Also, we have used X-ray crystallography to determine the structures of co-crystals of iron and Dps in varying proportions and compare the changes in these ligand-bound forms with respect to the apo-protein. The iron-loaded proteins of low, medium and high iron-bound forms were found to exhibit aspartate residues with alternate conformations, some of which could be directly linked to the sites of ferroxidation and iron entry. We conclude that the increased flexibility of aspartates in the presence of iron facilitates its movement from the entry site to the ferroxidaton site, and the two active sites are stabilized by the interactions of a conserved arginine residue R73.
机译：饥饿（DPS）下的DNA结合蛋白质是用于在细菌细胞中的铁氧化和储存的十二烷基聚纳米室。这些蛋白质具有大致球形结构，其中空心内部储存铁。通过对来自分枝杆菌的第二DPS蛋白在第二个DPS蛋白中的突变分析，我们已经鉴定了稳定铁进入和铁氧化位点之间的界面的残基。此外，我们已经使用了X射线晶体学，以确定不同比例的铁和DP的共晶的结构，并比较这些配体相对于apo-蛋白的变化。发现低，培养基和高铁染色形式的钢蛋白与交替构象的天冬氨酸残基表现出来，其中一些可以与铁氧化和铁进入的部位直接连接。我们得出结论，在铁的存在下，天冬氨酸的柔韧性促进其从进入部位到苯erroxidaton位点的运动，并且通过保守的精氨酸残基R73的相互作用稳定两个活性位点。

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