5I69

MBP-MamC magnetite-interaction component mutant-D70A

Summary for 5I69

• Entry DOI: 10.2210/pdb5i69/pdb
• Related PRD ID: PRD_900001
• Descriptor: Maltose-binding periplasmic protein,Tightly bound bacterial magnetic particle protein,Maltose-binding periplasmic protein, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: magnetotactic bacteria, mamc, biomineralization, magnetite, protein-mineral interaction, magnetite binding protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 1
• Total formula weight: 45585.29

Authors

Nudelman, H.,Tercedor, C.V.,Kolusheva, S.,Gonzalez, T.P.,Widdrat, M.,Grimberg, N.,Levi, H.,Nelkenbaum, O.,Davidove, G.,Faivre, D.,Jimenez-Lopez, C.,Zarivach, R. (deposition date: 2016-02-16, release date: 2016-03-23, Last modification date: 2024-01-10)

Primary citation

Nudelman, H.,Valverde-Tercedor, C.,Kolusheva, S.,Perez Gonzalez, T.,Widdrat, M.,Grimberg, N.,Levi, H.,Nelkenbaum, O.,Davidov, G.,Faivre, D.,Jimenez-Lopez, C.,Zarivach, R.
Structure-function studies of the magnetite-biomineralizing magnetosome-associated protein MamC.
J.Struct.Biol., 194:244-252, 2016

PubMed 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.

PubMed: 26970040
DOI: 10.1016/j.jsb.2016.03.001

Experimental method

X-RAY DIFFRACTION (2.7 Å)