Dr. Priya Ragunathan, PhD

Nanyang Technological University

School of Biological Sciences
60 Nanyang Drive
Singapore 637551

Email: rpriya@ntu.edu.sg

PhD Thesis:

Structural characterization of subunit b of the bacterial F1FO ATP synthase and the critical roles of conserved P-loop residues of the archaea A1AO-ATP synthase Subunit A. Degree in 2011

Publications:

  1. Rishikesan, S., Thaker, R. Y., Priya, R., Gayen, S., Manimekalai, M. S. S., Hunke, C., and Grüber, G. (2008) Spectroscopical identification of residues of subunit G of the yeast V-ATPase in its connection with subunit E. Mol. Mem. Biol. 25, 400-410

  2. Priya, R., Tadwal, V. S., Rössle, M., Gayen, S., Hunke, C., Peng, W. C., Torres, J., and Grüber, G. (2008) Low resolution structure of subunit b (b22-156) of Escherichia coli F1FO ATP synthase in solution and the b-d assembly. J. Bioenerg. Biomembr. 40, 245-255

  3. Priya, R., Biuković, G., Gayen, S., Vivekanandan, S., and Grüber, G. (2009) Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1FO ATP synthase. J. Bacteriology 191, 7538-7544

  4. Kumar, A., Manimekalai, M. S. S., Balakrishna, A. M., Priya, R., Biuković, G., Jeyakanthan, J., and Grüber, G. (2010) The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide-binding. J. Mol. Biol. 401, 892-905

  5. Priya, R., Kumar, A., Manimekalai, M. S. S., and Grüber, G. (2011) Conserved glycine residues in the P-loop of ATP synthases form a doorframe for nucleotide entrance. J. Mol. Biol. 413, 657-666

  6. Priya, R., Biuković, G., Manimekalai, M. S. S., Lim, J., Rao, S. P. S., and Grüber, G. (2013) Solution structure of subunit γ (γ1-204) of the Mycobacterium tuberculosis F-ATP synthase and the unique loop of γ165-178, representing a novel TB drug target. J. Bioenerg. Biomembr. 45, 121-129

  7. 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

  8. 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

  9. 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

  10. Gopal, P., Nartey, W., Ragunathan, P., Sarathy, J., Kaya, F., Yee, M., Setzer, C., Manimekalai, M.S.S., Dartois, V., Grüber, G. and Dick, T. (2017) Pyrazinoic acid inhibits mycobacterial coenzyme A biosynthesis by binding to aspartate decarboxylase PanD. ACS Infect Dis. 2017, 3, 807-819

  11. 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

  12. Bogdanović, N, Sundararaman, L., Kamariah, N., Tyagi, A., Bhushan, S., Ragunathan, P., Shin, J., Dick, T., and Grüber, G.* (2018) Structure and function of Mycobacterium-specific components of F-ATP synthase subunits α and ε. J. Struct. Biol. 280, 420-434

  13. Sarathy, J., Ragunathan, P., Shin, J., Cooper, C., Upton, A., Grüber, G.*, and Dick, T.* (2019) TBAJ-876 retains Bedaquiline’s activity against subunit c and ε of Mycobacterium tuberculosis F-ATP synthase. Antimicrob. Agents Chemother. 63, e01191-19

  14. Saw, W.-G.1, Wu, M.-L1, Ragunathan, P.1, Biuković, G, Lau, A.-M., Shin, J., Harikishore, A., Cheung, C.-Y., Hards, K., Sarathy, J. P., Bates, R. W., Cook, G. M. C., Dick, T.*, and Grüber, G.* (2019) Disrupting coupling within mycobacterial F-ATPsynthase subunit ε causes dysregulated energy production and cell wall biosynthesis. Sci. Rep. 9, 16759

  15. Kamariah, N., Ragunathan, P., Shin, J., Saw, W.-G., Wong, C.F., Dick, T., and Grüber, G.* (2020) Unique structural and mechanistic properties of mycobacterial F-ATP synthases: Implications for drug design. Prog. Biophys. Mol. Biol. 152, 64-73

  16. Sarathy, J., Ragunathan, P., Cooper, C., Upton, A., Grüber, G.*, and Dick, T.* (2020) TBAJ-876 displays Bedaquiline-like mycobactericidal potency without retaining the parental drug’s uncoupler activity. Antimicrob. Agents Chemother. 64, e01540-19

  17. Harikishore, A., Chong, S. S. M., Ragunathan, P., Bates, R. W., and Grüber, G.* (2020) Targeting the menaquinol binding loop of mycobacterial cytochrome bd oxidase. Mol. Div., doi: 10.1007/s11030-020-10034-0

  18. Gopal, P., Sarathy, J., Yee, Y., Ragunathan, P., Shin, J., Bhushan, S., Zhu, J., Akopian, T., Kandror, O., Lim, T.K., Gengenbacher, M., Lin, Q., Rubin, E.J., Grüber, G., and Dick, T. (2020) Pyrazinamide triggers degradation of its target aspartate decarboxylase. Nature Commun. 11, 1661

  19. Hotra, A., Ragunathan P., Ng, P.S., Seankongsuk, P., Harikishore, A., Sarathy, J.P., Saw, W.-G., Lakshmanan, U., Sae-Lao, P., Kalia, N.P., Shin, J., Kalyanasundaram, R., Anbarasu, S., Parthasarathy, K., Pradeep, C.N., Makhija, H., Dröge, P., Poulsen, A., Tan, J.H.L., Pethe, K., Dick, T., Bates, R.W., and Grüber, G.* (2020) Discovery of a novel Mycobacterial F-ATP synthase inhibitor and its potency in combination with diarylquinolines. Angewandte Chemie i.Ed, 132, 13397-13406

  20. Shin, J., Singal, B., Manimekalai, M.S.S., Chen, M.W., Ragunathan, P., and Grüber, G.* (2020) Atomic structure of, and valine binding to the regulatory ACT domain of the Mycobacterium tuberculosis Rel protein. FEBS J. 288, 2377-2397

  21. Wong, C.-F., Lau, A.-M., Harikishore, A., Saw, W.-G., Shin J., Ragunathan, P., Bhushan, S., Ngan, S. F. C., Sze, S. K., Bates, R.W., Dick, T., and Grüber, G.* (2021) A systematic assessment of mycobacterial F1-ATPase subunit ε’s role in latent ATPase hydrolysis. FEBS J. 288, 818-836

  22. Ragunathan, P., Cole, M., Latka, C., Aragaw, W.W., Hegde, P., Shin, J., Manimekalai, M.S.S., Rishikesan, S., Aldrich, C., Dick, T., and Grüber, G.* (2021) Mycobacterium tuberculosis PanD structure-function analysis and identification of a potent pyrazinoic acid-derived enzyme inhibitor. ACS Chem. Biol.16, 1030-1039

  23. Shin, J., Singal, B., Grüber, A., Wong, M.K.D., Ragunathan, P., and Grüber, G.* (2021) Atomic structure of the TGS domain of Rel protein from Mycobacterium tuberculosis and its interaction with deacylated tRNA. FEBS Lett. 595, 3006-3018

  24. Harikishore, A., Wong, C.-F., Ragunathan, P., Litty, D., Müller, V., and Grüber, G.* (2021) Targeting mycobacterial F-ATP synthase C-terminal α subunit interaction motif on rotary subunit γ. Antibiotics 10, 1456

  25. Harikishore, A., Saw, W.-G., Ragunathan, P., Litty, D., Dick, T., Müller, V., and Grüber, G.* (2022) Mutational analysis of mycobacterial F-ATP synthase subunit δ leads to a potent δ enzyme inhibitor. ACS Chem. Biol. 17, 529-535

  26. Ragunathan, P., Dick, T., and Grüber, G.* (2022) Anti-Mycobacterium abscessus activity of tuberculosis F-ATP synthase inhibitor GaMF1. Antimicrob. Agents and Chemother. 66, e0001822

  27. Shin, J., Harikishore, A., Wong, C.-F., Ragunathan, P., Dick, T., and Grüber, G.* (2022) Atomic solution structure of Mycobacterium abscessus F-ATP synthase subunit ε and identification of Ep1MabF1 as a targeted inhibitor. FEBS J. in press

  28. Saw, W.-G., Leow, C.Y., Harikishore, A., Shin, J., Cole, M., Aragaw, W.W., Ragunathan, P., Hegde, P., Aldrich, C.C., Dick, T., and Grüber, G.* (2022) Structural and mechanistic insights into Mycobacterium abscessus aspartate decarboxylase PanD and a pyrazinoic acid-derived inhibitor. ACS Infect. Dis., in press

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last update 10-Jun-2022