Structural highlights
FunctionD2JIV0_SINCO 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 PubMedFerritins are ubiquitous iron-binding proteins that are mainly related to iron storage, detoxification and innate immunity. Here, we present the crystal structure of a marine invertebrate ferritin from Sinonovacula constricta at a resolution of 1.98 A. The S. constricta ferritin (ScFer) possessed some structural similarities with vertebrate ferritins, and they shared a well-conserved architecture composed of five alpha-helical bundles that assembled into a cage-like structure with 24-subunits. The structure of ScFer also showed iron binding sites in the 3-fold channel, ferroxidase center, and putative nucleation sites. Further, electrostatic potential calculations suggested that the electrostatic gradient of the 3-fold channel could provide a guidance mechanism for iron entering the ferritin cavity. Crystallographic characterization of ferritin from Sinonovacula constricta.,Su C, Ming T, Wu Y, Jiang Q, Huan H, Lu C, Zhou J, Li Y, Song H, Su X Biochem Biophys Res Commun. 2020 Mar 26;524(1):217-223. doi:, 10.1016/j.bbrc.2020.01.069. Epub 2020 Jan 23. PMID:31983429[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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