6A4U

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

Summary for 6A4U

• Entry DOI: 10.2210/pdb6a4u/pdb
• Descriptor: Ferritin, 1,2-ETHANEDIOL, SULFATE ION, ... (6 entities in total)
• Functional Keywords: ferritin, crustacean, iron, ferroxidase site, nucleation site, metal binding protein
• Biological source: Marsupenaeus japonicus
• Total number of polymer chains: 6
• Total formula weight: 120841.39

Authors

Masuda, T.,Mikami, B.,Zang, J.,Zhao, G. (deposition date: 2018-06-21, release date: 2018-08-22, Last modification date: 2023-11-22)

Primary citation

Masuda, T.,Zang, J.,Zhao, G.,Mikami, B.
The first crystal structure of crustacean ferritin that is a hybrid type of H and L ferritin
Protein Sci., 27:1955-1960, 2018

PubMed 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.

PubMed: 30099791
DOI: 10.1002/pro.3495

Experimental method

X-RAY DIFFRACTION (1.16 Å)