6L56

Fe(II) loaded Tegillarca granosa ferritin

6L56 の概要

• エントリーDOI: 10.2210/pdb6l56/pdb
• 分子名称: Ferritin, FE (III) ION, FE (II) ION, ... (5 entities in total)
• 機能のキーワード: ferritin, copper, tegillarca granosa, structural genomics, center for eukaryotic structural genomics, cesg, oxidoreductase
• 由来する生物種: Tegillarca granosa (Malaysian cockle)
• タンパク質・核酸の鎖数: 24
• 化学式量合計: 485338.99

構造登録者

Jiang, Q.Q.,Su, X.R.,Ming, T.H.,Huan, H.S. (登録日: 2019-10-22, 公開日: 2019-11-13, 最終更新日: 2023-11-22)

主引用文献

Ming, T.H.,Jiang, Q.Q.,Huo, C.,Huan, H.S.,Wu, Y.,Su, C.,Qiu, X.,Lu, C.,Zhou, J.,Li, Y.,Han, J.,Zhang, Z.,Su, X.R.
Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa.
Front Mol Biosci, 9:800008-800008, 2022

PubMed Abstract: In addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu ions can also play crucial antibacterial roles in the blood clam, . However, the mechanism of interaction between iron and copper in recombinant ferritin (TgFer) remains to be investigated. In this study, we investigated the crystal structure of TgFer and examined the effects of Fe and Cu ions on the TgFer structure and catalytic activity. The crystal structure revealed that TgFer presented a typically 4-3-2 symmetry in a cage-like, spherical shell composed of 24 identical subunits, featuring highly conserved organization in both the ferroxidase center and the 3-fold channel. Structural and biochemical analyses indicated that the 4-fold channel of TgFer could be serviced as potential binding sites of metal ions. Cu ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe ions, possibly inhibiting the ferroxidase activity of TgFer. Our results present a structural and functional characterization of TgFer, providing mechanistic insight into the interactions between TgFer and both Fe and Cu ions.

PubMed: 35359603
DOI: 10.3389/fmolb.2022.800008

実験手法

X-RAY DIFFRACTION (1.85300580472 Å)