Magnetotaxis is a characteristic ability of some marine bacteria to sense and coordinate movement along the Earth`s magnetic field lines. Magnetotactic bacteria (MTB) are a diverse group of aquatic bacteria that have the magnetotaxis ability to navigate and align themselves along the geomagnetic field lines to a microoxic zone at the bottom of chemically stratified natural water. This special navigation is the result of a unique linear assembly of a specialized organelle, the magnetosome, which contains a biomineralized magnetic nanocrystal enveloped by a cytoplasmic membrane. By using the magnetosome chain, the MTB has an intricate phenotype of magnetotaxis.
The Magnetospirillum gryphiswaldense MSR-1 MGR0208 protein (MtxA) was suggested to play a role in the bacterial magnetotaxis due to its gene location in an operon encoding signal transduction genes. Since no homology is found for MtxA, and to better understand the role and function of MtxA in MTB’s magnetotaxis, we initiated structural and functional studies of MtxA via X-ray crystallography. Here, we present the successful expression, purification, crystallization and preliminary X-ray analysis of MtxAΔ1-24, a truncated polypeptide lacking the signal peptide.