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The first crystal structure of crustacean ferritin that is a hybrid type of H and L ferritin
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DOI：10.1002/pro.3495.png)
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Abstract
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<jats:title>Abstract</jats:title><jats:p>Ferritin, a ubiquitous iron storage protein, has a crucial role in innate immunity in arthropods, which have no adaptive immune system. Arthropods are thought to have two types of ferritin molecules: the secreted type and the cytosolic type. Here, we present the first crystal structure of ferritin from crustacean, kuruma prawn (<jats:italic>Marsupenaeus japonicus</jats:italic>), at 1.16 Å resolution. This shrimp ferritin (MjFer) is the cytosolic type, and its structure shows well‐conserved ferritin fold composed of a 4‐helix bundle that assembles into a cage‐like 24‐mer. The structure of MjFer was more similar to those of human and vertebrate ferritins than to that of the secreted‐type arthropod ferritin from an insect. MjFer possesses both a ferroxidase site and a nucleation site, which are the main characteristics of vertebrate H and L chain ferritins, respectively. The first crystal structure of crustacean ferritin, MjFer, has exceptionally high quality that provides the detailed structural information of metal moving pathway in ferritin.</jats:p>
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