s Structure Based Functional Annotation of Putative Conserved Proteins from Treponema pallidum: Search for a Potential Drug Target

Treponema pallidum, a Gram negative bacterium, causes chronic disease syphilis, a sexually transmitted disease. T. pallidum penetrates dermal micro abrasions or intact mucous membranes resulting in varieties of symptoms. The complete genome for T. pallidum was sequenced, which contains approximately 1,090 genes encoding approximately 1,041 proteins. These open reading frames account for a large number of hypothetical proteins (HPs) for which no pieces of experimental evidence are available. Being a virulent and not very well characterized organism, it is essential to analyze these HPs whose structure and function are not available in the protein data bank. Here, our aim is to predict structure and ultimately function of HPs using combination of modern bioinformatics tools. We successfully modeled the structures of six HPs with high accuracy, which possess endonuclease, NTP-transferase, transcription regulator and DNA-binding activities. We further performed virulence search to check their potential role in pathogenicity. Here, we performed an extensive structure analysis to get an insight into the function of a particular HP. We believe that these analyses expand our knowledge regarding the functional roles of HPs in the T. pallidum and provide an opportunity to validate novel potential drug targets.