Theoretical model of the structure of Glycolytic enzyme, Phosphoglycerate kinase C from Leishmania mexicana; transition from a continuous to discontinuous helix at the C-terminus and the role of GXXXG motif
5th International Conference on PARASITOLOGY & MICROBIOLOGY
July 12-13, 2018 Paris, France

Vidya Raghunathan

National Institute of Immunology, India

Scientific Tracks Abstracts: J Bacteriol Parasitol

Abstract:

Phosphoglycerate kinase C (PGKC) from the trypanosomatida, Leishmania is an important housekeeping enzyme whose 63 residue C-terminal extension is believed to be important in glycosome compartmentalisation. Structural studies with this enzyme have been experimentally very challenging. We sought to establish the three dimensional structure of residues 6-417 of PGKC_ L. Mexicana by homology modelling and biochemical data. Since PGKC of Leishmania and T.brucei are evolutionarily related and have high sequence homology the known structure of the PGKC_Tbrucei was used as template. We have created a .pdb library of individual fragments of the enzyme based on the Jpred secondary structure which can be useful for experts in the field of bioinformatics/protein modelling. Using chimera we have a final theoretical 3-dimensional model of L.Mexicana PGKC (residues 1-479) that enables visualization of the GXXXG motif in the enzyme fold. While supporting our biochemical data, the docking interactions reveal new aspects of the tertiary fold of PGKC. Various conjectures on PGKC�??s role in the glycosome, give crucial leads for further research.

Biography :

Vidya Raghunathan completed her Ph.D in Chemistry from Princeton University, USA and has been working in the National Institute of Immunology since 1991. She is currently the head of her laboratory working on the metabolic aspects of Leishmania from the perspective of structural biology of some key proteins. She has trained many students in her laboratory and is part of the mentorship programme in NII.

E-mail: vraghuna@nii.ac.in