The Structural Studies of the Bovine Respirasome, DUSP19 and PTP sigma

Abstract

Proteins play an important role in most living organism. Although the information need to life to go on is encoded by the DNA, the living process of life maintenance is carried out by proteins. They control cell division, metabolism, death and the flow information into and out of the cell. To know how cells work in living organism, we need proteins structure and its function. The question of proteins function is not a simple one to answer. A remarkable thing is that all function in charge of proteins are based on the twenty amino acids which can form a protein by covalent bonds. That is the reason why we studying proteins, their structure, molecular dynamics, structural composition and function. If we want to know the reason such as cancer, diabetes and aging, we have to understand what related proteins is, how these molecules fold, how complex proteins are assembled and how they function in macromolecule states. In this study, we report the 1) structural studies of the bovine respirasome , 2) structural studies of activity-modulating mutations of DUSP19, and 3) structural studies of protein tyrosine phosphatase sigma in the sulfenic acid form, using X-ray crystallography (2,3) and Cryo-EM (1) which currently used to understand three-dimensional structure of purified proteins. In first section, we discuss the new insight about the electron transport mechanism. We then discuss the cavity-mediated structural rearrangements which related to allosteric regulation. In the last section of this study, we discuss the novel possibility of structural regulation by cysteine oxidation.