TY - JOUR
T1 - Structure-function studies of the magnetite-biomineralizing magnetosome-associated protein MamC
AU - Nudelman, Hila
AU - Valverde-Tercedor, Carmen
AU - Kolusheva, Sofiya
AU - Perez Gonzalez, Teresa
AU - Widdrat, Marc
AU - Grimberg, Noam
AU - Levi, Hilla
AU - Nelkenbaum, Or
AU - Davidov, Geula
AU - Faivre, Damien
AU - Jimenez-Lopez, Concepcion
AU - Zarivach, Raz
N1 - Publisher Copyright:
© 2016.
PY - 2016/6/1
Y1 - 2016/6/1
N2 - 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.
AB - 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.
KW - Biomineralization
KW - Magnetotactic bacteria
KW - MamC
KW - Protein structure
KW - Structure-activity relationships
UR - http://www.scopus.com/inward/record.url?scp=84961156941&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2016.03.001
DO - 10.1016/j.jsb.2016.03.001
M3 - Article
AN - SCOPUS:84961156941
SN - 1047-8477
VL - 194
SP - 244
EP - 252
JO - Journal of Structural Biology
JF - Journal of Structural Biology
IS - 3
ER -