In silico structural and functional analyses of hypothetical proteins may unravel the hidden information seeded inside the protein sequence. This information could be utilized in finding new drug targets and drug designing. In the current study, we used different bioinformatics algorithms to conduct structural and functional annotations of a hypothetical protein in Mycobacterium leprae, ML-1369. In brief, at first the sequence analysis and secondary structure prediction were conducted and found that the studied hypothetical protein is a stable hydrophilic protein with a significant proportion of alpha helix and random coil. The protein was predicted to be a cytoplasmic protein. After that, we built the 3D model of the hypothetical protein using SWISS-MODEL from the complete amino acid sequence by homology modeling method. Then, we employed several quality and structural assessment programs such as ERRAT, Q-MEAN, ProSA, Procheck and found that the generated 3D model was structurally good and reliable. We also found that the protein contained the domain of unknown function (DUF) 387 and might belong to chromosomal condensation and segregation protein ScpB. STRING analysis also suggested the interaction of this protein with several others in cell division. The hypothetical protein is essential for the organism, although showed no homology to any human protein. Furthermore, KEGG analysis recommended the involvement of the protein in genetic information processing, environmental information processing, cellular processes and organisomal systems of M. leprae. The findings of the study will help better understanding of the functional protein network in the M. leprae that might lead to valuable drug development.
Hypothetical protein, Mycobacterium leprae, ML-1369, Cell division
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