Structural And Functional Studies Of Rv1674c

Mycobacterium tuberculosis is a chronic infectious disease, also known as Myco-bacterium tuberculosis (MTB, Mycobacterium tuberculosis) infection. The World Health Organization (WHO) reported that each year about 8 million new cases, and at least 300 million deaths caused. It is complicated to detect and treat TB because MTB can survive within the host for months to decades in an asymptomatic state. The mec-hanism of persistence of MTB is far from clearly understood.Adaptations to hypoxia play an important role in Mycobacterium tuberculosis pat-hogenesis. Recently, the MTB regulatory network based on 50 transcription factors has been described and has provided new insight into the physiological consequences of the regulatory programs induced by changes in oxygen availability. Adaptations to hypoxia are thought to play a prominent role in the persistence of MTB. In this net-work, Rv0324 is an important knot. It is predicted to activate another knot, KstR, which is a cholesterol degradation repressor. Rv0324 and KstR are both associated with the enduring hypoxic response (EHR), which is induced later but not in the initial response to hypoxia. Rv 1674c is a homologue of Rv0324,contains two domains: an N-terminal HTH ArsR-type DNA-binding domain and a C-terminal rhodanese domain.Rv1674c protein is presumed to be a transcription factor in M. tuberculosis, has some function about the transcription regulatory, wherein HTH Domain for binding DNA, RHOD as functional regions of the protein, play a major role in the transfer of a sulfur atom.The HTH structure maybe binding one or some DNA sequences that can play some protein functions, we start from this direction trying to find a DNA sequence with Rv 1674c protein combine to further reveal the protein’s function.And RHOD as functional domains in Rv1674c protein plays sulfur transfer function, through in vitro experiments can be a preliminary understanding of the functional activity of the protein.The research of MTB S-transferase enzyme only has few reports current. Protein crystallization by vapor diffusion method we first obtain the high-resolution crystal structure of Rv 1674c protein 2.05 A preliminary diffraction analysis showed that the crystals belong to space group P3221, parameters a=b=67.79A, c=174.54 A, a= β=90°,γ=120°, each crystal is composed of two protein molecules.