Two-dimensional crystals of carboxysome shell proteins recapitulate the hexagonal packing of three-dimensional crystals
Two-dimensional crystals of carboxysome shell proteins recapitulate the hexagonal packing of three-dimensional crystals
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DOI：
10.1002/pro.272
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发表时间：
2009-12-01
期刊：
影响因子：
8
通讯作者：
Yeager, Mark
中科院分区：
文献类型：
--
作者：
Dryden, Kelly A.;Crowley, Christopher S.;Yeager, Mark
细菌微室(BMC)是许多细菌中作为简单细胞器的大型胞内小体。它们是由多面体蛋白质壳包裹的关键酶组成的蛋白质结构。在以前的研究中，这些大的壳的组织已经从组成壳的蛋白质在三维(3D)晶体的背景下的二维(2D)层的保守堆积中推断出来。在这里，我们展示了当His标记的蛋白质在空气-水界面结合到镍相关的脂类分子的单层时，有序的、2D的羧基体壳蛋白晶体自发组装。2D晶体中的分子堆积概括了3D晶体中观察到的层状六角形薄片。这一结果强化了现有的BMC壳层分子设计模型。
Bacterial microcompartments (BMCs) are large intracellular bodies that serve as simple organelles in many bacteria. They are proteinaceous structures composed of key enzymes encapsulated by a polyhedral protein shell. In previous studies, the organization of these large shells has been inferred from the conserved packing of the component shell proteins in two-dimensional (2D) layers within the context of three-dimensional (3D) crystals. Here, we show that well-ordered, 2D crystals of carboxysome shell proteins assemble spontaneously when His-tagged proteins bind to a monolayer of nickelated lipid molecules at an air-water interface. The molecular packing within the 2D crystals recapitulates the layered hexagonal sheets observed in 3D crystals. The results reinforce current models for the molecular design of BMC shells.