The structure of PknB in complex with mitoxantrone, an ATP-competitive inhibitor, suggests a mode of protein kinase regulation in mycobacteria

FEBS Letters

Volumn 580, Issue 13, 2006, Pages 3018-3022

  Wehenkel, Annemarie ^a   Fernandez, Pablo ^a   Bellinzoni, Marco ^a   Catherinot, Vincent ^b   Barilone, Nathalie ^a   Labesse, Gilles ^b   Jackson, Mary ^a   Alzari, Pedro M ^a  

^a INSTITUT PASTEUR   (France)

^b CNRS   (France)

Author keywords

Back to back dimerization; Crystal structure; Drug design; Mycobacterium tuberculosis; Ser Thr protein kinase inhibitor complex

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTHRAQUINONE DERIVATIVE; BACTERIAL ENZYME; MITOXANTRONE; PKNB ENZYME; PROTEIN KINASE; UNCLASSIFIED DRUG; PKNB PROTEIN, MYCOBACTERIUM TUBERCULOSIS; PROTEIN SERINE THREONINE KINASE;

ARTICLE; BACTERIAL GROWTH; CANCER THERAPY; CELL GROWTH; COMPETITIVE INHIBITION; CRYSTAL STRUCTURE; CRYSTALLOGRAPHY; ENZYME REGULATION; MYCOBACTERIUM; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; CHEMISTRY; DIMERIZATION; DRUG ANTAGONISM; DRUG EFFECT; ENZYMOLOGY; METABOLISM; PROTEIN CONFORMATION;

CORYNEBACTERINEAE; MYCOBACTERIUM TUBERCULOSIS;

ADENOSINE TRIPHOSPHATE; DIMERIZATION; MITOXANTRONE; MYCOBACTERIUM TUBERCULOSIS; PROTEIN CONFORMATION; PROTEIN-SERINE-THREONINE KINASES;

EID: 33746058686     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.04.046     Document Type: Article

References (26)

1. Hunter T. Signaling-2000 and beyond. Cell 100 (2000) 113-127
2. Sassetti C.M., Boyd D.H., and Rubin E.J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 48 (2003) 77-84
3. Ortiz-Lombardia M., Pompeo F., Boitel B., and Alzari P.M. Crystal structure of the catalytic domain of the PknB serine/threonine kinase from Mycobacterium tuberculosis. J. Biol. Chem. 278 (2003) 13094-13100
4. Young T.A., Delagoutte B., Endrizzi J.A., Falick A.M., and Alber T. Structure of Mycobaterium tuberculosis PknB supports a universal activation mechanism for Ser/Thr protein kinases. Nat. Struct. Biol. 10 (2003) 168-174
5. Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T., Cerveñansky C., and 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 (2003) 1493-1508
6. Villarino A., Duran R., Wehenkel A., Fernandez P., England P., Brodin P., Cole S.T., Zimny-Arndt U., Jungblut P.R., Cerveñansky C., and Alzari P.M. Proteomic identification of M. tuberculosis protein kinase substrates: PknB recruits GarA, a FHA-containing protein, through activation loop-mediated interactions. J. Mol. Biol. 350 (2005) 953-963
7. Kang C.M., Abbott D.W., Park S.T., Dascher C.C., Cantley L.C., and Husson R.N. The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev. 19 (2005) 1692-1704
8. Cohen P. Protein kinases, the major drug targets of the 21st century?. Nat. Rev. Drug Discov. 1 (2002) 309-316
9. Noble M.E.M., Endicott J.A., and Johnson L.N. Protein kinase inhibitors: insights into drug design from structure. Science 303 (2004) 1800-1805
10. Rarey M., Wefing S., and Lengauer T. Placement of medium-sized molecular fragments into active sites of proteins. J. Comp. Aided Mol Des. 10 (1996) 41-54
11. Martin A., Camacho M., Portaels F., and Palomino J.-C. Resazurin microtiter assay plate testing of Mycobacterium tuberculosis susceptibilities to second-line drugs: rapid, simple, and inexpensive method. Antimicrob. Agents Chemotherap. 47 (2003) 3616-3619
12. CCP4, Collaborative Computational Project Number. Acta Cryst. D 50 (1994) 760-763
13. McCoy A.J., Grosse-Kunstleve R.W., Storoni L.C., and Read R.J. Likelihood-enhanced fast translation functions. Acta Cryst. D 61 (2005) 458-464
14. Brunger A.T., Adams P.D., Clore G.M., Gros P., Grosse-Kunstleve R.W., Jiang J.-S., Kuszewski J., Nilges M., Pannu N.S., Read R.J., Rice L.M., Simonson T., and Warren G.L. Crystallography & NMR system (CNS): a new software system for macromolecular structure determination. Acta Cryst. D 54 (1998) 905-921
15. Jones T.A., Zhou J.Y., Cowan S.W., and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A 47 (1991) 110-119
16. Glaser F., Pupko T., Paz I., Bell R.E., Bechor-Shental D., Martz E., and Ben-Tal N. ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 19 (2003) 163-164
17. Shenkenberg T.D., and Von Hoff D.D. Mitoxantrone: a new anticancer drug with significant clinical activity. Ann. Int. Med. 105 (1986) 67-81
18. Basra J., Wolf C.R., Brown J.R., and Patterson L.H. Evidence for human liver mediated free-radical formation by doxorubicin and mitoxantrone. Anticancer Drug Des. 1 (1985) 45
19. Jinsart W., Ternai B., and Polya G.M. Inhibition of myosin light chain kinase, cAMP-dependent protein kinase, protein kinase C and of plant Ca(2+)-dependent protein kinase by anthraquinones. Biol. Chem. Hoppe-Seyler 373 (1992) 903-910
20. Takeuchi N., Nakamura T., Takeuchi F., Hashimoto E., and Yamamura H. Inhibitory effect of mitoxantrone on activity of protein kinase C and growth of HL60 cells. J. Biochem. (Tokyo) 112 (1992) 762-767
21. Jackson M., Berthet F.-X., Otal I., Rauzier J., Martin C., Gicquel B., and Guilhot C. The Mycobacterium tuberculosis purine biosynthetic pathway: isolation and characterization of the purC and purL genes. Microbiology 142 (1996) 2439-2447
22. Dar A.C., Dever T.E., and Sicheri F. Higher-order substrate recognition of eIF2a by the RNA-dependent protein kinase PKR. Cell 122 (2005) 887-900
23. Dey M., Cao C., Dar A.C., Tamura T., Ozato K., Sicheri F., and Dever T.E. Mechanistic link between PKR dimerization, autophosphorylation and eIF2a substrate recognition. Cell 122 (2005) 901-913
24. Madec E., Laszkiewicz A., Iwanicki A., Obuchowski M., and Seror S. Characterization of a membrane-linked Ser/Thr protein kinase in Bacillus subtilis, implicated in developmental processes. Mol. Microbiol. 2 (2002) 571-586
25. Duran R., Villarino A., Bellinzoni M., Wehenkel A., Fernandez P., Boitel B., Cole S.T., Alzari P.M., and Cervenansky C. Conserved autophosphorylation pattern in activation loops and juxtamembrane regions of M. tuberculosis Ser/Thr protein kinases. Biophys. Biochem. Res. Commun. 333 (2005) 858-867
26. Traxler P., and Furet P. Strategies toward the design of novel and selective protein tyrosine kinase inhibitors. Pharmacol. Ther. 82 (1999) 195-206