Cation Diffusion Facilitator (CDF) protein family is a highly conserved metal ion efflux transporters family that maintains metal divalent cation homeostasis in all organisms. The members of the subfamily solute carrier (SLC30) are classified as zinc transporters that different mutations within them were shown to enhance or cause variety of diseases. For example, syndrome of hepatic cirrhosis, dystonia, polycythemia, hypermanganesemia and parkinsonism are caused by mutations in the manganese transporter ZnT-10. More specifically, the missense mutation L349P (1046 T>C) in ZnT-10 was shown to be related with hepatomegaly and dystonia. We use the magnetosome associated protein MamM cytosolic domain (C- terminal domain or CTD) from the magnetotactic bacteria strain Magnetospirillum gryphiswaldense MSR-1, a member of the CDF protein family, as a homolog model to study ZnT-10 L349P mutation. Magnetosomes are sub-cellular organelles in Magnetotactic bacteria (MTB) that biomineralize ~50 nm crystals of magnetite or greigite, and enable the MTB to orient themselves along geomagnetic fields. MamM transports Fe(II) into the magnetosome by exploiting the proton motive force and participate in magnetite formation. In this work, we made a structural model for ZnT-10 CTD. By comparing the structures we found the ZnT-10 L349 parallel amino acid in MamM CTD and started to characterize the structure-function relationship in the homolog mutation, MamM CTD M250P. This work enables better understanding of the mutation related diseases` mechanisms.
