EXTRACTION, PURIFICATION, AND SMALL-ANGLE X-RAY SCATTERING ANALYSIS OF THE YSXC GTPASE OF STAPHYLOCOCCUS AUREUS

Abstract

Study of the structures of various biological macromolecules is one of the main directions that are intensively developed using physical methods. Since proteins are an elementary unit of the structural and functional organization of a cell, the strategies for combating pathogenic microorganisms include the analysis of the bacterial protein synthesis apparatus and related systems. The extraction, purification, and small-angle X-ray scattering analysis of the structure of YsxC protein from the Staphylococcus aureus pathogenic bacterium are reported. This protein is involved in the cell growth and division processes, serves an energy-dependent factor, and participates in the assembly of large ribosome subunit. The structural study of this protein opens up a possibility of searching for small molecules capable of inhibiting its function. Since the structural variability of protein factors is higher than that of the conservative ribosome sites, their inhibition makes it possible to selectively affect a pathogenic microorganism.