7RVB
High resolution map of molecular chaperone Artemin
Summary for 7RVB
| Entry DOI | 10.2210/pdb7rvb/pdb |
| EMDB information | 24706 24707 |
| Descriptor | Ferritin (1 entity in total) |
| Functional Keywords | molecular chaperone artemin is a homolog of apoferritin, chaperone |
| Biological source | Artemia franciscana |
| Total number of polymer chains | 24 |
| Total formula weight | 627477.89 |
| Authors | Parvate, A.D.,Powell, S.M.,Brookreason, J.T.,Novikova, I.V.,Evans, J.E. (deposition date: 2021-08-18, release date: 2022-12-14, Last modification date: 2024-11-06) |
| Primary citation | Parvate, A.D.,Powell, S.M.,Brookreson, J.T.,Moser, T.H.,Novikova, I.V.,Zhou, M.,Evans, J.E. Cryo-EM structure of the diapause chaperone artemin. Front Mol Biosci, 9:998562-998562, 2022 Cited by PubMed Abstract: 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. PubMed: 36518848DOI: 10.3389/fmolb.2022.998562 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.04 Å) |
Structure validation
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