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

MPG-Autoren
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Valverde-Tercedor,  Carmen
Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Faivre,  Damien
Damien Faivre, Biomaterialien, Max Planck Institute of Colloids and Interfaces, Max Planck Society;

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Zitation

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.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002A-10B6-8
Zusammenfassung
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.