Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa
In addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu2+ ions can also play crucial antibacterial roles in the blood clam, Tegillarca granosa. However, the mechanism of interaction between iron and copper in...
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Frontiers Media S.A.
2022-03-01
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Online Access: | https://www.frontiersin.org/articles/10.3389/fmolb.2022.800008/full |
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author | Tinghong Ming Tinghong Ming Qinqin Jiang Qinqin Jiang Chunheng Huo Chunheng Huo Hengshang Huan Hengshang Huan Yan Wu Yan Wu Chang Su Xiaoting Qiu Chenyang Lu Chenyang Lu Jun Zhou Jun Zhou Ye Li Ye Li Jiaojiao Han Jiaojiao Han Zhen Zhang Zhen Zhang Xiurong Su Xiurong Su |
author_facet | Tinghong Ming Tinghong Ming Qinqin Jiang Qinqin Jiang Chunheng Huo Chunheng Huo Hengshang Huan Hengshang Huan Yan Wu Yan Wu Chang Su Xiaoting Qiu Chenyang Lu Chenyang Lu Jun Zhou Jun Zhou Ye Li Ye Li Jiaojiao Han Jiaojiao Han Zhen Zhang Zhen Zhang Xiurong Su Xiurong Su |
author_sort | Tinghong Ming |
collection | DOAJ |
description | In addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu2+ ions can also play crucial antibacterial roles in the blood clam, Tegillarca granosa. However, the mechanism of interaction between iron and copper in recombinant Tegillarca granosa ferritin (TgFer) remains to be investigated. In this study, we investigated the crystal structure of TgFer and examined the effects of Fe2+ and Cu2+ 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. Cu2+ ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe2+ 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 Fe2+ and Cu2+ ions. |
first_indexed | 2024-12-11T10:45:50Z |
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language | English |
last_indexed | 2024-12-11T10:45:50Z |
publishDate | 2022-03-01 |
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series | Frontiers in Molecular Biosciences |
spelling | doaj.art-3fe674f1825247bf9c2a86ae53cb32a92022-12-22T01:10:29ZengFrontiers Media S.A.Frontiers in Molecular Biosciences2296-889X2022-03-01910.3389/fmolb.2022.800008800008Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosaTinghong Ming0Tinghong Ming1Qinqin Jiang2Qinqin Jiang3Chunheng Huo4Chunheng Huo5Hengshang Huan6Hengshang Huan7Yan Wu8Yan Wu9Chang Su10Xiaoting Qiu11Chenyang Lu12Chenyang Lu13Jun Zhou14Jun Zhou15Ye Li16Ye Li17Jiaojiao Han18Jiaojiao Han19Zhen Zhang20Zhen Zhang21Xiurong Su22Xiurong Su23State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaCollege of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaCollege of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaCollege of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, ChinaZhejiang Collaborative Innovation Center for High Value Utilization of Byproducts from Ethylene Project, Ningbo Polytechnic College, Ningbo, ChinaCollege of Food and Pharmaceutical Sciences, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaState Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, ChinaSchool of Marine Science, Ningbo University, Ningbo, ChinaIn addition to its role as an iron storage protein, ferritin can function as a major detoxification component in the innate immune defense, and Cu2+ ions can also play crucial antibacterial roles in the blood clam, Tegillarca granosa. However, the mechanism of interaction between iron and copper in recombinant Tegillarca granosa ferritin (TgFer) remains to be investigated. In this study, we investigated the crystal structure of TgFer and examined the effects of Fe2+ and Cu2+ 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. Cu2+ ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe2+ 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 Fe2+ and Cu2+ ions.https://www.frontiersin.org/articles/10.3389/fmolb.2022.800008/fullblood clam Tegillarca granosaferritincrystal structureFe2+ ionCu2+ ioncatalytic activity |
spellingShingle | Tinghong Ming Tinghong Ming Qinqin Jiang Qinqin Jiang Chunheng Huo Chunheng Huo Hengshang Huan Hengshang Huan Yan Wu Yan Wu Chang Su Xiaoting Qiu Chenyang Lu Chenyang Lu Jun Zhou Jun Zhou Ye Li Ye Li Jiaojiao Han Jiaojiao Han Zhen Zhang Zhen Zhang Xiurong Su Xiurong Su Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa Frontiers in Molecular Biosciences blood clam Tegillarca granosa ferritin crystal structure Fe2+ ion Cu2+ ion catalytic activity |
title | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa |
title_full | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa |
title_fullStr | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa |
title_full_unstemmed | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa |
title_short | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa |
title_sort | structural insights into the effects of interactions with iron and copper ions on ferritin from the blood clam tegillarca granosa |
topic | blood clam Tegillarca granosa ferritin crystal structure Fe2+ ion Cu2+ ion catalytic activity |
url | https://www.frontiersin.org/articles/10.3389/fmolb.2022.800008/full |
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