• PknB
• References
• Slides

References

1. Young, T.A., Delagoutee, B., Endrizzi, J.A., Falcik, A.M. & Alber, T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10, 168–174 (2003).

2. Biondi, R.M. & Nebreda, A.R. Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions. Biochem. 372, 1-13 (2003).

3. Fernandez, P., Saint-Joanis, B., Barilone, N., Jackson, M., Gicquel, B., Cole, S.T. & Alzari, P.M. The Ser/Thr Protein Kinase PknB Is Essential for Sustaining Mycobacterial Growth. J.  Bacteriol.188(22), 7778–7784 (2006).

4. Dasgupta, A., Datta, P., Kundu, M. & Basu, J. The serine/threonine kinase PknB of Mycobacteriu tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division. Microbiology. 152, 493-504 (2006).

5. PDB ID: 1MRU

   Young, T.A., Delagoutee, B., Endrizzi, J.A., Falcik, A.M. & Alber, T. Structure of Mycobacterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10, 168–174 (2003).

6. Knight, J.D.R., Qian, B., Baker, D. & Kothary, R. Conservation, Variability and the Modeling of Active Protein Kinases. PLoS ONE 2(10): e982.Doi:10.1371/journal.pone.0000982

7. Gay, L.M., Ng, H. & Alber, T. A Conserved Dimer and Global Conformational Changes in the Structure of apo-PknE Ser/Thr Protein Kinase from Mycobacterium tuberculosis. J. Mol. Biol. 360, 409–420 (2006).

8. Villarino, A., Duran, R., Wehenkel, A., Fernandez, P., England, P., Brodlin, P., Cole, S.T., Zimny-Arndt, U., Junglut, P.R., Cervenansky, C. & Alzari, P.M. Proteomic Identification of M. tuberculosis Protein Kinase Substrates: PknB Recruits GarA, a FHA Domain-containing Protein, Through Activation Loop-mediated Interactions. J. Mol. Biol. 350, 953-963 (2005).

9. Boitel, B., Ortiz-Lombardía, M., Durán, R., Pompeo, F., Cole, S.T., Cerveñansky, C. & Alzari, P.M. PknB kinase activity is regulated by phosphorylation in two Thr residues  and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis. Mol. Microbiol. 49(6), 1493-1508 (2003).

10. PDB ID: 2H34

   Gay, L.M., Ng, H. & Alber, T. A Conserved Dimer and Global Conformational Changes in the Structure of apo-PknE Ser/Thr Protein Kinase from Mycobacterium tuberculosis. J. Mol. Biol. 360, 409–420 (2006).