The first crystal structure of crustacean ferritin that is a hybrid type of H and L ferritin

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  • Taro Masuda
    Laboratory of Food Quality Design and Development, Division of Agronomy and Horticultural Science Graduate School of Agriculture, Kyoto University Kyoto 611‐0011 Japan
  • Jiachen Zang
    College of Food Science & Nutritional Engineering, Beijing Key Laboratory of Functional Food from Plant Resources China Agricultural University Beijing, 100083 China
  • Guanghua Zhao
    College of Food Science & Nutritional Engineering, Beijing Key Laboratory of Functional Food from Plant Resources China Agricultural University Beijing, 100083 China
  • Bunzo Mikami
    Laboratory of Applied Structural Biology, Division of Applied Life Sciences Graduate School of Agriculture, Kyoto University Kyoto Japan

説明

<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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