Dr. Wilson Nartey, PhD

Arnie Charbonneau Cancer Institute

University of Calgary
Canada

PhD Thesis:

Mechanistic insights into Escherichia coli Alkyl Hydroperoxide Reductase complex formation. Degree in 2016

 

Publications:

  1. Dip, P. V., Kamariah, N., Manimekalai, M. S. S., Nartey, W., Balakrishna, A. M., Eisenhaber, F., Eisenhaber, B. and Grüber, G. (2014) Structure, mechanism and ensemble formation of the Alkylhydroperoxide Reductase subunits AhpC and AhpF from Escherichia coli. Acta Crystallogr. D70, 2848-2862

  2. Dip, P. V.1, Kamariah, N.1, Nartey, W.1, Beushausen, C., Kostyuchenko, V. A., Ng, T. S., Lok, S. M., Saw, W. G., Eisenhaber, F., Eisenhaber, B. and Grüber, G. (2014) Key roles for the Escherichia coli AhpC C-terminus in assembly and catalysis of alkylhydroperoxide reductase, an enzyme essential for the alleviation of oxidative stress. Biochim. Biophys. Acta 1837, 1932-1943

  3. Kamariah, N., Manimekalai, M. S. S., Nartey, W., Eisenhaber, F., Eisenhaber, B. and Grüber, G. (2015) Crystallographic and solution studies of NAD+- and NADH-bond Alkylhydroperoxide Reductase subunit F (AhpF) from Escherichia coli provide insight into sequential enzymatic steps. Biochim. Biophys. Acta-Bioenergetics 1847, 1139-1152

  4. 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

  5. Kamariah, N.1, Nartey, W.1, Eisenhaber, B., Eisenhaber, F., and Grüber, G.* (2016) Low resolution solution structure of an enzymatic active AhpC10:AhpF2 ensemble of the Escherichia coli Alkylhydroperoxide Reductase. J. Struct. Biol. 193, 13-22

  6. Kumar, A., Balakrishna, A. M.1, Nartey, W.1, Manimekalai, M. S. S., and Grüber, G. (2016) Redox chemistry of Mycobacterium tuberculosis alkylhydroperoxide reductase E (AhpE): Structural and mechanistic insight into a mycoredoxin-1 independent reductive pathway of AhpE via mycothiol. Free Rad. Biol. Med. 97, 588-601

  7. Kumar, A., Nartey, W., Shin, J., Manimekalai, M. S. S., and Grüber, G. (2017) Structural and mechanistic insights into Mycothiol Disulphide Reductase and the Mycoredoxin-1-alkylhydroperoxide reductase E assembly of Mycobacterium tuberculosis. Biochim. Biophys. Acta-General Subject 1861, 2354-2366

  8. 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 Letters 591, 2323-2337

  9. 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

  10. Pan, A., Balakrishna, A.M., Nartey, W., Kohlmeier, A., Dip, P.V., Bhushan, S., Grüber, G.* (2018) Atomic structure and enzymatic insights into the vancomycin-resistant Enterococcus faecalis (V583) alkylhydroperoxide reductase subunit C. Free Rad. Biol. Med. 115, 252-265

  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. Kamariah, N., Huber, R.G., Nartey, W., Bhushan, S., Bond, P.J. and Grüber, G.* (2019) Structure and subunit arrangement of Mycobacterial F1FO ATP synthase and novel features of the unique mycobacterial subunit δ. J. Struct. Biol. 207, 199-208

1 (Authors have equal contribution)


last update 24-Jul-2019