8ED3
Structure of a nanoparticle with icosahedral symmetry
8ED3 の概要
| エントリーDOI | 10.2210/pdb8ed3/pdb |
| EMDBエントリー | 28027 |
| 分子名称 | Designed I3-01 icosahedron (1 entity in total) |
| 機能のキーワード | protein design, nanoparticle, de novo protein |
| 由来する生物種 | Thermotoga maritima MSB8 |
| タンパク質・核酸の鎖数 | 60 |
| 化学式量合計 | 1299635.04 |
| 構造登録者 | |
| 主引用文献 | McCarthy, S.,Gonen, S. Improved interface packing and design opportunities revealed by CryoEM analysis of a designed protein nanocage. Heliyon, 8:e12280-e12280, 2022 Cited by PubMed Abstract: Symmetric protein assemblies play important roles in nature which makes them an attractive target for engineering. symmetric protein complexes can be created through computational protein design to tailor their properties from first principles, and recently several protein nanocages have been created by bringing together protein components through hydrophobic interactions. Accurate experimental structures of newly-developed proteins are essential to validate their design, improve assembly stability, and tailor downstream applications. We describe the CryoEM structure of the nanocage I3-01, at an overall resolution of 3.5 Å. I3-01, comprising 60 aldolase subunits arranged with icosahedral symmetry, has resisted high-resolution characterization. Some key differences between the refined structure and the original design are identified, such as improved packing of hydrophobic sidechains, providing insight to the resistance of I3-01 to high-resolution averaging. Based on our analysis, we suggest factors important in the design and structural processing of new assemblies. PubMed: 36590526DOI: 10.1016/j.heliyon.2022.e12280 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.5 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






