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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 Cu(2+) ions can also play crucial antibacterial roles in the blood clam, Tegillarca granosa. However, the mechanism of interaction between iron and copper i...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8961696/ https://www.ncbi.nlm.nih.gov/pubmed/35359603 http://dx.doi.org/10.3389/fmolb.2022.800008 |
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author | Ming, Tinghong Jiang, Qinqin Huo, Chunheng Huan, Hengshang Wu, Yan Su, Chang Qiu, Xiaoting Lu, Chenyang Zhou, Jun Li, Ye Han, Jiaojiao Zhang, Zhen Su, Xiurong |
author_facet | Ming, Tinghong Jiang, Qinqin Huo, Chunheng Huan, Hengshang Wu, Yan Su, Chang Qiu, Xiaoting Lu, Chenyang Zhou, Jun Li, Ye Han, Jiaojiao Zhang, Zhen Su, Xiurong |
author_sort | Ming, Tinghong |
collection | PubMed |
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 Cu(2+) 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 Fe(2+) and Cu(2+) 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(2+) ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe(2+) 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(2+) and Cu(2+) ions. |
format | Online Article Text |
id | pubmed-8961696 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-89616962022-03-30 Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa Ming, Tinghong Jiang, Qinqin Huo, Chunheng Huan, Hengshang Wu, Yan Su, Chang Qiu, Xiaoting Lu, Chenyang Zhou, Jun Li, Ye Han, Jiaojiao Zhang, Zhen Su, Xiurong Front Mol Biosci Molecular Biosciences 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(2+) 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 Fe(2+) and Cu(2+) 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(2+) ions appear to bind preferentially with the 3-fold channel as well as ferroxidase site over Fe(2+) 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(2+) and Cu(2+) ions. Frontiers Media S.A. 2022-03-11 /pmc/articles/PMC8961696/ /pubmed/35359603 http://dx.doi.org/10.3389/fmolb.2022.800008 Text en Copyright © 2022 Ming, Jiang, Huo, Huan, Wu, Su, Qiu, Lu, Zhou, Li, Han, Zhang and Su. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Molecular Biosciences Ming, Tinghong Jiang, Qinqin Huo, Chunheng Huan, Hengshang Wu, Yan Su, Chang Qiu, Xiaoting Lu, Chenyang Zhou, Jun Li, Ye Han, Jiaojiao Zhang, Zhen Su, Xiurong Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa |
title | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa
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title_full | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa
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title_fullStr | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa
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title_full_unstemmed | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa
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title_short | Structural Insights Into the Effects of Interactions With Iron and Copper Ions on Ferritin From the Blood Clam Tegillarca granosa
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title_sort | structural insights into the effects of interactions with iron and copper ions on ferritin from the blood clam tegillarca granosa |
topic | Molecular Biosciences |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8961696/ https://www.ncbi.nlm.nih.gov/pubmed/35359603 http://dx.doi.org/10.3389/fmolb.2022.800008 |
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