Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments

Structural characterization of encapsulated ferritin provides insight into iron storage in bacterial nanocompartments
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封装铁蛋白的结构表征有助于深入了解细菌纳米室中的铁储存

DOI:
10.1101/063495
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发表时间:
2016
期刊:
--
影响因子:
--
通讯作者:
He D
He D
中科院分区:
--
文献类型:
--
作者:
He D

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铁蛋白是普遍存在的蛋白质,可氧化铁并将铁储存在蛋白质壳内,以保护细胞免受氧化损伤。我们表征了铁蛋白超家族新成员的结构和功能,该成员被隔离在封装蛋白衣壳内。我们表明,这种封装的铁蛋白(EncFtn)具有两个主要的α螺旋,它们以金属依赖性方式组装,在二聚体界面形成亚铁氧化酶中心。 EncFtn 采用开放式十聚体结构,其拓扑结构与其他铁蛋白不同。虽然 EncFtn 充当亚铁氧化酶,但它不能矿化铁。相反,封装蛋白壳与铁结合,但不具有酶活性,我们证明 EncFtn 必须容纳在封装蛋白内才能储存铁。这种封装蛋白纳米室广泛分布在细菌和古细菌中,代表了一类独特的铁存储系统,其中铁的氧化和矿化分布在两种蛋白质之间。DOI:http://dx.doi.org/10.7554/eLife.18972.001
Ferritins are ubiquitous proteins that oxidise and store iron within a protein shell to protect cells from oxidative damage. We have characterized the structure and function of a new member of the ferritin superfamily that is sequestered within an encapsulin capsid. We show that this encapsulated ferritin (EncFtn) has two main alpha helices, which assemble in a metal dependent manner to form a ferroxidase center at a dimer interface. EncFtn adopts an open decameric structure that is topologically distinct from other ferritins. While EncFtn acts as a ferroxidase, it cannot mineralize iron. Conversely, the encapsulin shell associates with iron, but is not enzymatically active, and we demonstrate that EncFtn must be housed within the encapsulin for iron storage. This encapsulin nanocompartment is widely distributed in bacteria and archaea and represents a distinct class of iron storage system, where the oxidation and mineralization of iron are distributed between two proteins.DOI:http://dx.doi.org/10.7554/eLife.18972.001
DOI: 10.1006/jsbi.1999.4118
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