YfdX: Difference between revisions

YfdX weighs around 42kDa and is suggested to be a dimer in solution (Lee, Hye Seon, et al.). It has 10-186 residues from its total 199 amino acids (Lee, Hye Seon, et al.). It is composed of six α-helices, one 310-helix, and three β-strands. These arrange into three subdomains: a four helical bundle, and antiparallel β-sheet, and two helical bundles (Lee, Hye Seon, et al.). The importance of YfdX is that it plays a major role in Salmonella susceptibility to two β-lactam antibiotics, penicillin G and carbenicillin (Lee, Hye Seon, et al.). Without the YfdX protein the Salmonella virulence was enhanced. One specific type of YfdX protein is <scene name='81/814058/Sty3178/3'>STY3178</scene>. This comes from a multidrug resistant strain of Salmonella Typhi (Saha, P., Manna, C., Das, S., & Ghosh, M. (2016)). The multidrug resistant strains of S. Typhi. have been reported to be resistant to antibiotics such as ciprofloxacin, rifampin, ampicillin, etc. (Saha, P., Manna, C., Das, S., & Ghosh, M. (2016)). The structure of STY3178 was found in a study to be a well folded and predominately α-helical protein containing β-sheets elements (Saha, P., Manna, C., Das, S., & Ghosh, M. (2016)). STY3178 is existing in a trimetric oligomerization state in solution. (Saha, P., Manna, C., Das, S., & Ghosh, M. (2016)). Its ability to bind to antibiotics was found to demonstrate that different small antibiotics are capable of binding to STY3178 such as ciprofloxacin, rifampin, and ampicillin (Saha, P., Manna, C., Das, S., & Ghosh, M. (2016)). Studies show that the binding of ciprofloxacin binding is stronger than rifampin flowed by ampicillin (Saha, P., Manna, C., Das, S., & Ghosh, M. (2016)). This is important to note because if a patient were to come down with typhoid fever and had the STY3178 protein it would be best to see which antibiotic would bind best to the STY3178 protein.