Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: 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
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2022
Materias:
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
_version_ 1784677653868969984
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
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 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
work_keys_str_mv AT mingtinghong structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT jiangqinqin structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT huochunheng structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT huanhengshang structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT wuyan structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT suchang structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT qiuxiaoting structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT luchenyang structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT zhoujun structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT liye structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT hanjiaojiao structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT zhangzhen structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa
AT suxiurong structuralinsightsintotheeffectsofinteractionswithironandcopperionsonferritinfromthebloodclamtegillarcagranosa