7USN

Crystal structure of ferritin 1 from Caenorhabditis elegans, FTN-1

7USN の概要

• エントリーDOI: 10.2210/pdb7usn/pdb
• 分子名称: Ferritin, GLYCEROL, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: ferroxidase, oxidoreductase
• 由来する生物種: Caenorhabditis elegans
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 313833.15

構造登録者

Malcolm, T.R.,Maher, M.J.,Mubarak, S.S.M. (登録日: 2022-04-25, 公開日: 2023-04-26, 最終更新日: 2024-05-22)

主引用文献

Mubarak, S.S.M.,Malcolm, T.R.,Brown, H.G.,Hanssen, E.,Maher, M.J.,McColl, G.,Jameson, G.N.L.
Biochemical Characterization of Caenorhabditis elegans Ferritins.
Biochemistry, 62:1484-1496, 2023

PubMed Abstract: The nematode contains genes for two types of ferritin ( and ) that express FTN-1 and FTN-2. We have expressed and purified both proteins and characterized them by X-ray crystallography, cryo-electron microscopy, transmission electron microscopy, dynamic light scattering, and kinetically by oxygen electrode and UV-vis spectroscopy. Both show ferroxidase activity, but although they have identical ferroxidase active sites, FTN-2 is shown to react approximately 10 times faster than FTN-1, with L-type ferritin character over longer time periods. We hypothesize that the large variation in rate may be due to differences in the three- and four-fold channels into the interior of the protein 24-mer. FTN-2 is shown to have a wider entrance into the three-fold channel than FTN-1. Additionally, the charge gradient through the channel of FTN-2 is more pronounced, with Asn and Gln residues in FTN-1 replaced by Asp and Glu residues in FTN-2. Both FTN-1 and FTN-2 have an Asn residue near the ferroxidase active site that is a Val in most other species, including human H ferritin. This Asn residue has been observed before in ferritin from the marine pennate diatom Pseudo-mitzchia multiseries. By replacing this Asn residue with a Val in FTN-2, we show that the reactivity decreases over long time scales. We therefore propose that Asn106 is involved in iron transport from the ferroxidase active site to the central cavity of the protein.

PubMed: 37014173
DOI: 10.1021/acs.biochem.3c00005

実験手法

X-RAY DIFFRACTION (1.789 Å)