International Journal Bioautomation (Sep 2012)
In silico Comparative Modeling of PapA1 and PapA2 Proteins Involved in Mycobacterium Tuberculosis Sulfolipid-1 Biosynthesis Pathway
Abstract
Tuberculosis is one of the most serious health problems, as globally; around 2 billion or one third of the world's total population has been infected with Mycobacterium tuberculosis. Mycobacterium tuberculosis is a unique among bacterial pathogens in that it displays a wide array of complex lipids and lipoglycans on its cell surface. One such glycolipid, sulfolipid-1 (SL-1), is the most sulfatide, consists of a trehalose core, four fatty acyl groups, and a sulfate ester. Several proteins involved in SL-1 biosynthesis have been identified, the enzymes that acylate the T2S core to form SL1278 and SL-1, and the biosynthetic order of these acylation reactions, are unknown. Here we studied the in silico identification of PapA2 and PapA1, proteins responsible for the sequential acylation of T2S to form SL1278 and are essential for SL-1 biosynthesis, by applying different bioinformatics tools. Benchmark, of 3 different homology modeling programs Modeller, Swiss-Model (Deep View), and ESyPred3D, has been performed used to transform the alignment to a 3D model. The 3D structures of targeted proteins were evaluated by evaluation tools, ANOLEA and Verify3D. It is concluded that in SL-1 biosynthesis pathway, PapA1 and PapA2 proteins could be used as drug target, drug lead design and to find out the other proteins involved in this pathway that not yet have been identified and may be used to the cure of tuberculosis infection.
