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The first crystal structure of crustacean ferritin that is a hybrid type of H and L ferritin
Author(s) -
Masuda Taro,
Zang Jiachen,
Zhao Guanghua,
Mikami Bunzo
Publication year - 2018
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3495
Subject(s) - ferritin , biology , arthropod , cytosol , hemolymph , biochemistry , vertebrate , ceruloplasmin , chemistry , gene , enzyme , ecology
Abstract 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 ( Marsupenaeus japonicus ), 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.