Reprogramming an ATP-driven protein machine into a light-gated nanocage.
Reprogramming an ATP-driven protein machine into a light-gated nanocage.
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DOI：
10.1038/nnano.2013.242
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发表时间：
2013-12
影响因子：
38.3
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中科院分区：
文献类型：
--
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天然蛋白质组装体具有许多复杂的结构和功能，可以制造纳米级的储存容器、马达和泵。受这些系统的启发，蛋白质单体已经被设计成自组装成超分子结构，包括对称的，金属模板和笼状结构。然而，蛋白质机器的复杂性使得很难创建具有定义结构和可控功能的组件。在这里，我们报告的蛋白质组装已被工程作为光控纳米容器的功能。我们发现，腺苷-5 ′-三磷酸（ATP）驱动的II组伴侣蛋白，类似于一个内置盖子的桶，可以重新编程打开和关闭不同频率的光照射。通过将基于光可切换偶氮苯的分子设计到结构中，偶氮苯部分中原子间距离的光触发变化能够驱动蛋白质组装体的大规模构象变化。组装体的不同状态可以用单粒子低温电子显微镜观察到，并且纳米笼可以用于捕获和释放非天然货物。类似的用光改变原子距离的策略可以用来制造其他可控的纳米级机器。
Natural protein assemblies have many sophisticated architectures and functions, creating nanoscale storage containers, motors and pumps. Inspired by these systems, protein monomers have been engineered to self-assemble into supramolecular architectures including symmetrical, metal-templated and cage-like structures. The complexity of protein machines, however, has made it difficult to create assemblies with both defined structures and controllable functions. Here we report protein assemblies that have been engineered to function as light-controlled nanocontainers. We show that an adenosine-5′-triphosphate (ATP)-driven group II chaperonin, which resembles a barrel with a builtin lid, can be reprogrammed to open and close on illumination with different frequencies of light. By engineering photoswitchable azobenzene-based molecules into the structure, light-triggered changes in interatomic distances in the azobenzene moiety are able to drive large-scale conformational changes of the protein assembly. The different states of the assembly can be visualized with single particle cryo-electron microscopy, and the nanocages can be used to capture and release non-native cargos. Similar strategies switching atomic distances with light could be used to build other controllable nanoscale machines.
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