DESCRIPTION OF LAB RESEARCH WORK
The research group of Prof. Dr. G. Grüber at the School of Biological Sciences, NTU, is recognized for its expertise in determining the relationships between the structure and mechanism(s) of mycobacterial proteins like the Rel protein, ATPases, F-ATP synthases, in particular the F-ATP synthase from Mycobacterium tuberculosis (Mtb), the protein ensemble of the antioxidant defense of Mtb as well as key viral proteins. In order to get insight into the mechanism of these complexes, techniques like SAXS, X-ray crystallography, NMR-spectroscopy and electron microscopy are used. Biophysical techniques are used, to study protein-protein interactions, protein-ligand and protein-drug binding. His team extended successfully microbiology tools to study the potency of compounds on mycobacterial strains. The group is very experienced in cloning, production and purification of mycobacterial and viral proteins.
|Saw Wuan Geok
|Wong Chui Fann
- Drug Discovery for Emerging Infectious Diseases
- The variety of antioxidant defense ensembles in pathogenic bacteria to tackle reactive oxygen species
- Structural Dynamics of Virus Proteins in Solution
- Nartey, W., Basak, S., Kamariah, N., Manimekalai, M. S. S., Robson, S., Wagner, G., Eisenhaber, B., Eisenhaber, F., and Grüber, G. (2015) NMR studies reveal a novel grab and release mechanism necessary for efficient catalysis of the bacterial 2-Cys peroxiridoxin machinery. FEBS J., 282, 4620-4638.
- Cs, J. H., Sielaff, H., Nadeem, A., Svanborg, C. and Grüber, G. (2015) The molecular motor F-ATP synthase is targeted by the tumoricidal protein HAMLET. J. Mol. Biol. 427, 1866-1874.
- Saw, W. G., Tria, G., Grüber, A., Manimekalai, M. S. S., Zhao, Y., Chandramohan, A., Anand, G. S., Matsui, T., Weiss, T., Vasudevan, S. and Grüber, G. (2015) Structural insight and flexibility features of NS5 proteins from all four serotypes of Dengue virus in solution. Acta Crystallogr. D71, 2309-2327.
- Hotra, A., Suter, M., Biuković, G., Ragunathan, P., Kundu, S., Dick, T. and Grüber, G. (2016) Deletion of a unique loop in the mycobacterial F-ATP synthase γ subunit sheds light in its inhibitory role in ATP hydrolysis driven H+-pumping. FEBS J. 283, 1947-1961.
- Kumar, A., Balakrishna, A., Nartey, W., Manimekalai, M.S.S. and Grüber, G. (2016) Redox chemistry of Mycobacterium tuberculosis 1-Cys peroxiredoxin AhpE: Structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of AhpE via mycothiol. Free Rad. Biol. & Med. 97, 588-601.
- Wong, C.F., Shin, J., Manimekalai, M.S.S., Saw, W.G., Zhan, Y., Bhushan, S. Kumar, A., Ragunathan, P. and Grüber, G. (2017) The uniqueness of AhpC of the mycobacterial antioxidant defense system and its interaction with its reducing partner Thioredoxin-C. Sci. Rep. 7, 5159.
- Singal, B., Balakrishna, A., Nartey, W., Manimekalai, M.S.S., Jeyakanthan, J. and Grüber, G. (2017) Crystallographic and solution structure of the N-terminal domain of the Rel protein from Mycobacterium tuberculosis. FEBS Lett. 591, 2323-2337.
- Ragunathan, P, Sielaff, H., Sundararaman, L., Biuković, G., Manimekalai, M.S.S., Singh, D., Kundu, S., Wohland, T., Frasch, W., Dick, T. and Grüber, G. (2017) The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation. J. Biol. Chem. 292, 11262-11279.
- Saw, W. G., Pan, A., Manimekalai, M.S.S. and Grüber, G. (2017) Structural features of Zika virus non-structural proteins 3 and -5 and its individual domains in solution as well as insights into NS3 inhibition. Antiviral Res. 141, 73-90.
- Shin, J., Ragunathan, P., Sundararaman, L., Nartey, W., Kundu, S., Manimekalai, M.S.S., Bogdanović, N., Dick, T. and Grüber, G. (2018) The NMR solution structure of Mycobacterium tuberculosis F-ATP synthase subunit ε provides new insight into energy coupling inside the rotary engine. FEBS J. 285, 1111-1128.