Structural highlights
FunctionQ8WQM8_ARTSF Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.[RuleBase:RU361145] Publication Abstract from PubMedThe protein artemin acts as both an RNA and protein chaperone and constitutes over 10% of all protein in Artemia 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 A 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. Cryo-EM structure of the diapause chaperone artemin.,Parvate AD, Powell SM, Brookreson JT, Moser TH, Novikova IV, Zhou M, Evans JE Front Mol Biosci. 2022 Nov 28;9:998562. doi: 10.3389/fmolb.2022.998562. , eCollection 2022. PMID:36518848[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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