Our laboratory is focused on the elucidation of protein’s structure and function. To do so, lab members utilize various techniques available, ranging from Circular Dichroism to Macromolecular Crystallography.
The research in the lab is focused on two major topics: Magnetosome-related proteins, and effectors of the type III secretion system in pathogenic bacteria.
Structural biology aims to understand the chemistry, interactions and basic biological functions governed by the three-dimensional structure of macromolecules. Knowledge of the three-dimensional 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. Similarly, protein-ligand interactions are crucial in many biological processes with implications for drug targeting, gene expression, and biomineralization. X-ray crystallography and cryo-EM are the most prolific techniques for structural analysis of proteins and protein complexes. Using X-ray crystallography, cryo-EM reconstruction and additional techniques such as NMR and SAXS, we can now realize the high-resolution range, enabling a full coverage understanding of macromolecules and their interactions.
Magnetosome related 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. A large number of the proteins involved in magnetosome formation are of unknown function. Magnetite crystals formed by magnetotactic bacteria have a high potential for nano- and biotechnological applications, which require specifically-designed particle surfaces of distinct shape and size. Using a biomimetic approach, we can use the purified proteins, possibly mutated, to design and control the magnetite crystals, for many uses including protein tags and fluorophores. For commercial use, magnetite crystals with a permanent, stable, magnetic dipole moment at room temperature and with a specific size can be designed.
Cation diffusion facilitator (CDF) proteins
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 trans-membrane 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 the structure-function relationships of the CDF protein family.
The laboratory is also involved in performing structural and functional collaborations with various labs both in BGU and around the world to promote structural understanding.