Structural basis of enzyme encapsulation into a bacterial nanocompartment
Structural basis of enzyme encapsulation into a bacterial nanocompartment
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DOI：
10.1038/nsmb.1473
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发表时间：
2008-09-01
影响因子：
16.8
通讯作者：
Ban, Nenad
中科院分区：
文献类型：
--
作者：
Sutter, Markus;Boehringer, Daniel;Ban, Nenad
划分是生活的一个重要组织特征。它发生在不同水平的复杂性，从真核细胞器和细菌的微区室，由酶组装形成的分子反应室。酶在分子区室中包封的结构基础知之甚少。在这里，我们表明，使用X射线晶体学，生物化学和EM实验，一个广泛的保守的细菌蛋白质家族，linocin样蛋白，形成大的组件，作为一个最小的隔间包装酶的功能。我们将这种壳形成蛋白称为“壳蛋白”。在3.1埃分辨率下测定的来自海栖热袍菌的这种颗粒的晶体结构显示，60个单体拷贝组装成直径为240埃的薄的二十面体壳。该纳米区室的内部排列有保守的结合位点，用于作为参与氧化应激反应的酶的C-末端延伸存在的短多肽标签。
Compartmentalization is an important organizational feature of life. It occurs at varying levels of complexity ranging from eukaryotic organelles and the bacterial microcompartments, to the molecular reaction chambers formed by enzyme assemblies. The structural basis of enzyme encapsulation in molecular compartments is poorly understood. Here we show, using X-ray crystallographic, biochemical and EM experiments, that a widespread family of conserved bacterial proteins, the linocin-like proteins, form large assemblies that function as a minimal compartment to package enzymes. We refer to this shell-forming protein as 'encapsulin'. The crystal structure of such a particle from Thermotoga maritima determined at 3.1-angstrom resolution reveals that 60 copies of the monomer assemble into a thin, icosahedral shell with a diameter of 240 angstrom. The interior of this nanocompartment is lined with conserved binding sites for short polypeptide tags present as C-terminal extensions of enzymes involved in oxidative-stress response.