Murthy M R N

Molecular Biophysics Unit
Research Areas: 
Macromolecular crystallography
Research Highlights: 

Professor Murthy's work is mainly in the field of macromolecular crystallography, and the work in his laboratory has focussed on elucidating the structures and function of a large number of proteins, enzymes and their mutants. The main projects of this research group are: (1) Viral crystallography of two isometric ss-RNA plant viruses - the sesbania mosaic virus and the physalis mottle virus (2) Elucidation of three dimensional structures of three proteins from the malarial parasite Plasmodium falciparum - triosephosphate isomerase, adenylosuccinate synthase and hypoxanthine guanine phosphoribosyl transferase. (3) Many enzymes and proteins from Salmonella typhimurium have been structurally and biochemically elucidated. These include several enzymes involved in propionate and propanediol metabolism - methylisocitrate lyase, methylcitrate synthase, acetate kinase, propionate kinase and threonine deaminase. Apart from these, structures of the native and ligand complexes of pyridoxal phosphate dependent enzymes actetylornithine aminotransferase, D-serine deaminase, D-cysteine desulfhydrase, arginine decarboxylase from Salmonella typhimurium have also been determined and related to their function. Structures a few other enzymes, adenylosuccinate synthase, propanol dehydrogenase, a mutarotase and several proteins such as SurE, YnaF, Yda that are essential for the survival of Salmonella typhimurium under environmental stress have been determined. SurE has been used as a model protein to investigate the significance of domain swapping interactions in protein symmetry and function. (4) The structure and function of the pyridoxal phosphate dependent enzyme serinehydroxymethyl transferase from Bacillus stearothermophilus has been extensively investigated. (5) The most recent work carried out by this group in collaboration with Rik Wierenga is on the structure and function of SCP2-like thiolases of prokaryotes.

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