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-Structure paper
タイトル | Structural Characterization of Native and Modified Encapsulins as Nanoplatforms for in Vitro Catalysis and Cellular Uptake. |
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ジャーナル・号・ページ | ACS Nano, Vol. 11, Issue 12, Page 12796-12804, Year 2017 |
掲載日 | 2017年12月26日 |
著者 | Rindia M Putri / Carolina Allende-Ballestero / Daniel Luque / Robin Klem / Katerina-Asteria Rousou / Aijie Liu / Christoph H-H Traulsen / W Frederik Rurup / Melissa S T Koay / José R Castón / Jeroen J L M Cornelissen / |
PubMed 要旨 | Recent years have witnessed the emergence of bacterial semiorganelle encapsulins as promising platforms for bio-nanotechnology. To advance the development of encapsulins as nanoplatforms, a ...Recent years have witnessed the emergence of bacterial semiorganelle encapsulins as promising platforms for bio-nanotechnology. To advance the development of encapsulins as nanoplatforms, a functional and structural basis of these assemblies is required. Encapsulin from Brevibacterium linens is known to be a protein-based vessel for an enzyme cargo in its cavity, which could be replaced with a foreign cargo, resulting in a modified encapsulin. Here, we characterize the native structure of B. linens encapsulins with both native and foreign cargo using cryo-electron microscopy (cryo-EM). Furthermore, by harnessing the confined enzyme (i.e., a peroxidase), we demonstrate the functionality of the encapsulin for an in vitro surface-immobilized catalysis in a cascade pathway with an additional enzyme, glucose oxidase. We also demonstrate the in vivo functionality of the encapsulin for cellular uptake using mammalian macrophages. Unraveling both the structure and functionality of the encapsulins allows transforming biological nanocompartments into functional systems. |
リンク | ACS Nano / PubMed:29166561 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 11.4 - 28.3 Å |
構造データ | EMDB-3608: EMDB-3609: EMDB-3612: EMDB-3613: EMDB-3614: EMDB-3615: EMDB-3616: |
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