Domain Analysis of Fatty Acid Synthase Protein (NP_217040) from Mycobacterium tuberculosis H37Rv -- A Bioinformatics Study.
Different domains of fatty acid synthase ( FAS) protein of Mycobacterium tuberculosis H37Rv, involved in mycolic acid synthesis were analyzed using various bioinformatics tools. Based on different database searches (CDD and Pfam), FAS protein of Mycobacterium tuberculosis was grouped into eight domains, five of which showed close similarity with pdb templates (1MLA, 1IQ6A, 2BMOA, and 1J3NA). Based on the PSI blast analysis, 3D structures of only five domains were predicted using MODELLER software, and loop modeling was done for only those regions that were predicted as loops by predict protein server. Compared to the original structure, the loop modeled structure showed a lower DOPE score value for FAS protein. The X-ray determined templates that were used for predicting the 3D structure suggest that, FAS protein has "Malonyl-coenzyme A-Hydratase-Nitrobenzene dioxygenase-3-oxoacyl-(acp) synthase" activity. Accuracy of the prediction of 3D structure of different domains of FAS protein was further validated by Ramachandran plot and PROCHECK (G-value).[1]References
- Domain Analysis of Fatty Acid Synthase Protein (NP_217040) from Mycobacterium tuberculosis H37Rv -- A Bioinformatics Study. K V, R., Wagle, K., Deshmukh, S. J. Biomol. Struct. Dyn. (2007) [Pubmed]
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