6NLU
Circularly permuted Haliangium ochraceum BMC-H
6NLU の概要
| エントリーDOI | 10.2210/pdb6nlu/pdb |
| 分子名称 | circularly permuted BMC-H (2 entities in total) |
| 機能のキーワード | bacterial microcompartment, structural protein |
| 由来する生物種 | Haliangium ochraceum 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 21118.21 |
| 構造登録者 | |
| 主引用文献 | Ferlez, B.,Sutter, M.,Kerfeld, C.A. A designed bacterial microcompartment shell with tunable composition and precision cargo loading. Metab. Eng., 54:286-291, 2019 Cited by PubMed Abstract: Microbes often augment their metabolism by conditionally constructing proteinaceous organelles, known as bacterial microcompartments (BMCs), that encapsulate enzymes to degrade organic compounds or assimilate CO. BMCs self-assemble and are spatially delimited by a semi-permeable shell made up of hexameric, trimeric, and pentameric shell proteins. Bioengineers aim to recapitulate the organization and efficiency of these complex biological architectures by redesigning the shell to incorporate non-native enzymes from biotechnologically relevant pathways. To meet this challenge, a diverse set of synthetic biology tools are required, including methods to manipulate the properties of the shell as well as target and organize cargo encapsulation. We designed and determined the crystal structure of a synthetic shell protein building block with an inverted sidedness of its N- and C-terminal residues relative to its natural counterpart; the inversion targets genetically fused protein cargo to the lumen of the shell. Moreover, the titer of fluorescent protein cargo encapsulated using this strategy is controllable using an inducible tetracycline promoter. These results expand the available set of building blocks for precision engineering of BMC-based nanoreactors and are compatible with orthogonal methods which will facilitate the installation and organization of multi-enzyme pathways. PubMed: 31075444DOI: 10.1016/j.ymben.2019.04.011 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.607 Å) |
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