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-Structure paper
タイトル | Cryo-EM structure of the diapause chaperone artemin. |
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ジャーナル・号・ページ | Front Mol Biosci, Vol. 9, Page 998562, Year 2022 |
掲載日 | 2022年11月28日 |
![]() | Amar D Parvate / Samantha M Powell / Jory T Brookreson / Trevor H Moser / Irina V Novikova / Mowei Zhou / James E Evans / ![]() |
PubMed 要旨 | The protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in cysts during diapause. However, its mechanistic details remain elusive since no high- ...The protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in cysts during diapause. However, its mechanistic details remain elusive since no high-resolution structure of artemin exists. Here we report the full-length structure of artemin at 2.04 Å resolution. The cryo-EM map contains density for an intramolecular disulfide bond between Cys22-Cys61 and resolves the entire C-terminus extending into the core of the assembled protein cage but in a different configuration than previously hypothesized with molecular modeling. We also provide data supporting the role of C-terminal helix F towards stabilizing the dimer form that is believed to be important for its chaperoning activity. We were able to destabilize this effect by placing a tag at the C-terminus to fully pack the internal cavity and cause limited steric hindrance. |
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手法 | EM (単粒子) |
解像度 | 1.91 - 2.56 Å |
構造データ | ![]() EMDB-24145: Structure of commercially purchased Apoferritin EMDB-24706, PDB-7rvb: ![]() EMDB-24707: High resolution map of molecular chaperone Artemin with C term His Tag |
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![]() | CHAPERONE / Molecular chaperone Artemin is a homolog of apoferritin |