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  Structure-function studies of the magnetite-biomineralizing magnetosome-associated protein MamC

Nudelman, H., Valverde-Tercedor, C., Kolusheva, S., Gonzalez, T. P., Widdrat, M., Grimberg, N., et al. (2016). Structure-function studies of the magnetite-biomineralizing magnetosome-associated protein MamC. Journal of Structural Biology, 194(3), 244-252. doi:10.1016/j.jsb.2016.03.001.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-10B6-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-BCDA-2
Genre: Journal Article

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 Creators:
Nudelman, Hila, Author
Valverde-Tercedor, Carmen1, Author              
Kolusheva, Sofiya, Author
Gonzalez, Teresa Perez, Author
Widdrat, Marc, Author
Grimberg, Noam, Author
Levi, Hilla, Author
Nelkenbaum, Or, Author
Davidov, Geula, Author
Faivre, Damien1, Author              
Jimenez-Lopez, Concepcion, Author
Zarivach, Raz, Author
Affiliations:
1Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863290              

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Free keywords: biomineralization, magnetotactic bacteria, MamC, protein structure, 29 structure-activity relationships
 Abstract: Magnetotactic bacteria are Gram-negative bacteria that navigate along geomagnetic fields using the magnetosome, an organelle that consists of a membrane-enveloped magnetic nanoparticle. Magnetite formation and its properties are controlled by a specific set of proteins. MamC is a small magnetosome-membrane protein that is known to be active in iron biomineralization but its mechanism has yet to be clarified. Here, we studied the relationship between the MamC magnetite-interaction loop (MIL) structure and its magnetite interaction using an inert biomineralization protein-MamC chimera. Our determined structure shows an alpha-helical fold for MamC-MIL with highly charged surfaces. Additionally, the MamC-MIL induces the formation of larger magnetite crystals compared to protein-free and inert biomineralization protein control experiments. We suggest that the connection between the MamC-MIL structure and the protein’s charged surfaces is crucial for magnetite binding and thus for the size control of the magnetite nanoparticles.

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 Dates: 2016-03-102016-06
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: -
 Identifiers: DOI: 10.1016/j.jsb.2016.03.001
BibTex Citekey: Nudelman2016
 Degree: -

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Title: Journal of Structural Biology
  Abbreviation : J. Struct. Biol.
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 194 (3) Sequence Number: - Start / End Page: 244 - 252 Identifier: ISSN: 1047-8477