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Erschienen in:
2015 | OriginalPaper | Buchkapitel
In-Silico Structural Analysis of SoxF Protein Through Molecular Modelling and Protein-Protein Docking from Hydrogenophilus thermoluteolus: An Approach to Understand the Molecular Mechanism of Thiosulfate Oxidation
verfasst von : Sujay Ray, Angshuman Bagchi
Erschienen in: Information Systems Design and Intelligent Applications
Verlag: Springer India
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Abstract
Microbial redox reactions of inorganic sulphur compounds play vital role for recycling of sulphur to maintain environmental sulphur balance. These important reactions are carried out by enzyme system encoded by sox operon. Central player of sulphur oxidation process is SoxY–Z protein complex. Thermophilic beta-proteobacterium-Hydrogenophilus thermoluteolus, oxidizes sulphur compounds including thiosulfate with the help of proteins encoded by sox operon. Protein SoxF having sulfide dehydrogenase activity has the ability to reactivate the inactivated SoxY–Z complex. Till date no structural details are available for SoxF protein from H. thermoluteolus. In present work, homology modeling has been used to build 3D structures of SoxY, SoxZ and SoxF of H. thermoluteolus. 3D structure of SoxY–Z–F complex was obtained by ClusPro2.0. Amino acid residues responsible for protein-protein interaction were identified. Interactions in SoxY–Z–F were found to be mediated through hydrogen bonding. Probable biophysical mechanism of the interactions of SoxF with SoxY–Z complex has been identified.