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-Structure paper
タイトル | Improved interface packing and design opportunities revealed by CryoEM analysis of a designed protein nanocage. |
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ジャーナル・号・ページ | Heliyon, Vol. 8, Issue 12, Page e12280, Year 2022 |
掲載日 | 2022年12月14日 |
![]() | Stephen McCarthy / Shane Gonen / ![]() |
PubMed 要旨 | 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 ...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. |
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手法 | EM (単粒子) |
解像度 | 3.5 - 4.2 Å |
構造データ | EMDB-28027, PDB-8ed3: ![]() EMDB-28028: I3-01 in an expanded conformation ![]() EMDB-28029: I3-01 map refined in C1 |
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![]() | DE NOVO PROTEIN / Protein design / nanoparticle |