Background

Structural biology aims to understand the chemistry, interactions and basic biological functions governed by the three-dimensional structure of macromolecules. Knowledge of the 3-D structure of a protein can provide enormous basic scientific insight into the function of that protein, facilitating elucidation of its biochemical function and its interactions with other proteins, RNA, DNA, or membranes in the cell. X-ray crystallography and cryo-EM are the most prolific techniques for the structural analysis of proteins and protein complexes. Using X-ray crystallography and cryo-EM, we can now realize to the high-resolution range, up to atomic or even electronic details, enabling a full coverage understanding of macromolecules and their interactions.

Current Projects

1. Structural studies of magnetosome associated proteins. Magnetotactic bacteria are a phylogenetically and morphologically diverse group of microorganisms that share an ability to create magnetosomes, biomineral organelles that sense geomagnetic fields and aid the bacteria to align themselves accordingly. The magnetosome organelle comprises aligned 30-50 nm iron oxide magnetite crystals, surrounded by a lipid bilayer membrane vesicle. There are several types of magnetosome-forming proteins all encoded by genes within a genomic island common to magnetotactic bacteria. These proteins include a set of incorporated membrane proteins that facilitate vesicle formation, vesicle localization and iron transport and a set of proteins that control magnetite formation and size. In my lab, we are tackling the structure-function relationships of these proteins.

2. Structural studies of cation diffusion facilitators (CDF), a special family of cation transporters. Cation diffusion facilitator (CDF) proteins constitute a group of heavy metal ion efflux transporters that participate in metal ion homeostasis and can be found in all domains of life. Members of the CDF protein family – functional in their dimeric form and comprising a transmembrane domain (TMD) and a cytoplasmic C-terminal domain (CTD) – exploit the proton motive force to transport cytoplasmic divalent metal cations (e.g., Cd, Co, Fe, Mn, Ni, and Zn). Several debilitating human diseases, including type II diabetes, Parkinsonism and dystonia, and senescence, are known to be caused by mutations in human CDF proteins (SLC30A1-10/ZnT1-10). In my lab, we are studying cation discrimination and regulation via the biochemical studies of CDFs.

3. As a member of the Faculty of Natural Sciences at BGU, the lab will serve as a core facility and will be involved in protein structure determination and structural studies of other proteins.

Nudelman H., Lee Y., Hung Y., Kolusheva S., Upcher A., Chen Y., Chen J., Sue S. and Zarivach R. (2018) Understanding the biomineralization role of magnetite-interacting components (MICs) from magnetotactic bacteria. Front. Microbiol. 9:2480.

Uebe R., Keren-Khadmy N., Zeytuni N., Katzmann E., Navon Y., Davidov G., Bitton R., Plitzko JM., Schüler D. and Zarivach R. (2018) The dual role of MamB in magnetosome membrane assembly and magnetite biomineralization. Mol. Micro., 107(4):542-557.

Nudelman H., Gonzalez TP., Kolusheva S., Widdrat M., Reichel V., Peigneux A., Davidov G., Bitton R., Faivre D., López C.J. and Zarivach R. (2018) The importance of the helical structure of a MamC-derived magnetite-interacting peptide for its function in magnetite formation. Acta Crystallogr D Biol Crystallogr. 74(Pt 1):10-20.

Barber-Zucker S., Shaanan B. and Zarivach R. (2017) Transition metal binding selectivity in proteins and its correlation with the phylogenomic classification of the cation diffusion facilitator protein family. Sci Rep. 7(1):16381.

Ph.D. Weizmann Institute of Science, 2005.