Modeling,molecular docking,probing catalytic binding mode of acetyl-CoA malate synthase G in Brucella melitensis 16M |
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Authors: | Pradeepkiran Jangampalli Adi Nanda Kumar Yellapu Bhaskar Matcha |
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Institution: | 1. Division of Animal Biotechnology, Department of Zoology, Sri Venkateswara University, Tirupati 517502, Andhra Pradesh, India;2. Biomedical Informatics Centre, Vector Control Research Centre, Puducherry 605006, India |
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Abstract: | There are enormous evidences and previous reports standpoint that the enzyme of glyoxylate pathway malate synthase G (MSG) is a potential virulence factor in several pathogenic organisms, including Brucella melitensis 16M. Where the lack of crystal structures for best candidate proteins like MSG of B. melitensis 16M creates big lacuna to understand the molecular pathogenesis of brucellosis. In the present study, we have constructed a 3-D structure of MSG of Brucella melitensis 16M in MODELLER with the help of crystal structure of Mycobacterium tuberculosis malate synthase (PDB ID: 2GQ3) as template. The stereo chemical quality of the restrained model was evaluated by SAVES server; remarkably we identified the catalytic functional core domain located at 4th cleft with conserved catalytic amino acids, start at ILE 59 to VAL 586 manifest the function of the protein. Furthermore, virtual screening and docking results reveals that best leadmolecules binds at the core domain pocket of MSG catalytic residues and these ligand leads could be the best prospective inhibitors to treat brucellosis. |
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Keywords: | Malate synthase G Catalytic function Modeling Virtual screening Docking |
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