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Structure prediction and analysis of MxaF from obligate,facultative and restricted facultative methylobacterium
Authors:Raghvendra Pratap Singh  Ram Nageena Singh  Manish K Srivastava  Alok Kumar Srivastava  Sudheer Kumar  Ramesh Chandra Dubey  Arun Kumar Sharma
Affiliation:1Microbial Genomics Lab, National Bureau of Agriculturally Important Microorganisms, Kusmaur, Maunath Bhanjan, Uttar Pradesh-275101, India;2Department of Botany and Microbiology, Gurukul Kangri University, Haridwar, Uttrakhand-249404, India
Abstract:
Methylobacteria are ubiquitous in the biosphere which are capable of growing on C1 compounds such as formate, formaldehyde,methanol and methylamine as well as on a wide range of multi-carbon growth substrates such as C2, C3 and C4 compounds due tothe methylotrophic enzymes methanol dehydrogenase (MDH). MDH is performing these functions with the help of a key proteinmxaF. Unfortunately, detailed structural analysis and homology modeling of mxaF is remains undefined. Hence, the objective ofthis research is the characterization and three dimensional modeling of mxaF protein from three different methylotrophs by usingI-TASSER server. The predicted model were further optimize and validate by Profile 3D, Errat, Verifiy3-D and PROCHECK server.Predicted and best evaluated models have been successfully deposited to PMDB database with PMDB ID PM0077505, PM0077506and PM0077507. Active site identification revealed 11, 13 and 14 putative functional site residues in respected models. It may play amajor role during protein-protein, and protein-cofactor interactions. This study can provide us an ab-initio and detail information tounderstand the structure, mechanism of action and regulation of mxaF protein.
Keywords:Methylobacteria   mxaF protein   homology modeling   functional site
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