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

Hila Nudelman, Carmen Valverde-Tercedor, Sofiya Kolusheva, Teresa Perez Gonzalez, Marc Widdrat, Noam Grimberg, Hilla Levi, Or Nelkenbaum, Geula Davidov, Damien Faivre, Concepcion Jimenez-Lopez, Raz Zarivach

Research output: Contribution to journalArticlepeer-review

34 Scopus citations

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.

Original languageEnglish
Pages (from-to)244-252
Number of pages9
JournalJournal of Structural Biology
Volume194
Issue number3
DOIs
StatePublished - 1 Jun 2016

Keywords

  • Biomineralization
  • Magnetotactic bacteria
  • MamC
  • Protein structure
  • Structure-activity relationships

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