9G3H
Circularly permuted lumazine synthase twisted tube with no gap between between double strands
これはPDB形式変換不可エントリーです。
9G3H の概要
| エントリーDOI | 10.2210/pdb9g3h/pdb |
| EMDBエントリー | 50999 |
| 分子名称 | 6,7-dimethyl-8-ribityllumazine synthase (1 entity in total) |
| 機能のキーワード | protein cage, protein engineering, self-assembly, geometry, helical reconstruction, bionanotechnology, polymorphism, pentamer, de novo protein |
| 由来する生物種 | Aquifex aeolicus VF5 詳細 |
| タンパク質・核酸の鎖数 | 100 |
| 化学式量合計 | 1746593.40 |
| 構造登録者 | |
| 主引用文献 | Koziej, L.,Fatehi, F.,Aleksejczuk, M.,Byrne, M.J.,Heddle, J.G.,Twarock, R.,Azuma, Y. Dynamic Assembly of Pentamer-Based Protein Nanotubes. Acs Nano, 19:8786-8798, 2025 Cited by PubMed Abstract: Hollow proteinaceous particles are useful nanometric containers for delivery and catalysis. Understanding the molecular mechanisms and the geometrical theory behind the polymorphic protein assemblies provides a basis for designing ones with the desired morphology. As such, we found that a circularly permuted variant of a cage-forming enzyme, lumazine synthase, cpAaLS, assembles into a variety of hollow spherical and cylindrical structures in response to changes in ionic strength. Cryogenic electron microscopy revealed that these structures are composed entirely of pentameric subunits, and the dramatic cage-to-tube transformation is attributed to the moderately hindered 3-fold symmetry interaction and the imparted torsion angle of the building blocks, where both mechanisms are mediated by an α-helix domain that is untethered from the native position by circular permutation. Mathematical modeling suggests that the unique double- and triple-stranded helical arrangements of subunits are optimal tiling patterns, while different geometries should be possible by modulating the interaction angles of the pentagons. These structural insights into dynamic, pentamer-based protein cages and nanotubes afford guidelines for designing nanoarchitectures with customized morphology and assembly characteristics. PubMed: 39993171DOI: 10.1021/acsnano.4c16192 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.44 Å) |
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