User menu

Allosteric Mechanism of Pyruvate Kinase from Leishmania mexicana Uses a Rock and Lock Model

Bibliographic reference Morgan, Hugh P. ; McNae, Iain W. ; Nowicki, Matthew W. ; Hannaert, Véronique ; Michels, Paulus ; et. al. Allosteric Mechanism of Pyruvate Kinase from Leishmania mexicana Uses a Rock and Lock Model. In: Journal of Biological Chemistry, Vol. 285, no. 17, p. 12892-8 (2010)
Permanent URL http://hdl.handle.net/2078.1/33947
  1. Fenton Aron W., Allostery: an illustrated definition for the ‘second secret of life’, 10.1016/j.tibs.2008.05.009
  2. Laskowski Roman A., Gerick Fabian, Thornton Janet M., The structural basis of allosteric regulation in proteins, 10.1016/j.febslet.2009.03.019
  3. Jardetzky Oleg, Protein dynamics and conformational transitions in allosteric proteins, 10.1016/s0079-6107(96)00010-7
  4. Daily Michael D., Gray Jeffrey J., Local motions in a benchmark of allosteric proteins, 10.1002/prot.21300
  5. Consler, J. Biol. Chem., 263, 2794 (1988)
  6. Lee J. Ching, Modulation of allostery of pyruvate kinase by shifting of an ensemble of microstates, 10.1111/j.1745-7270.2008.00445.x
  7. Ernest Isabelle, Callens Mia, Opperdoes Fred R., Michels Paul A.M., Pyruvate kinase of Leishmania mexicana mexicana Cloning and analysis of the gene, overexpression in Escherichia coli and characterization of the enzyme, 10.1016/0166-6851(94)90133-3
  8. Collins Richard A., Kelly Sharon M., Price Nicholas C., Fothergill-Gilmore Linda A., Muirhead Hilary, Ligand-induced conformational changes in wild-type and mutant yeast pyruvate kinase, 10.1093/protein/9.12.1203
  9. Hannaert Véronique, Yernaux Cédric, Rigden Daniel J, Fothergill-Gilmore Linda A, Opperdoes Fred R, Michels Paul A.M, The putative effector-binding site ofLeishmania mexicanapyruvate kinase studied by site-directed mutagenesis, 10.1016/s0014-5793(02)02374-8
  10. Ikeda Yoshitaka, Tanaka Takehiko, Noguchi Tamio, Conversion of Non-allosteric Pyruvate Kinase Isozyme into an Allosteric Enzyme by a Single Amino Acid Substitution, 10.1074/jbc.272.33.20495
  11. Pendergrass David C., Williams Rachel, Blair James B., Fenton Aron W., Mining for allosteric information: Natural mutations and positional sequence conservation in pyruvate kinase, 10.1080/15216540500531705
  12. Lindsley J. E., Rutter J., Whence cometh the allosterome?, 10.1073/pnas.0604452103
  13. Valentini Giovanna, Chiarelli Laurent R., Fortin Riccardo, Dolzan Manuela, Galizzi Alessandro, Abraham Donald J., Wang Changqing, Bianchi Paola, Zanella Alberto, Mattevi Andrea, Structure and Function of Human Erythrocyte Pyruvate Kinase : MOLECULAR BASIS OF NONSPHEROCYTIC HEMOLYTIC ANEMIA, 10.1074/jbc.m202107200
  14. Rigden Daniel J, Phillips Simon E.V, Michels Paul A.M, Fothergill-Gilmore Linda A, The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity 1 1Edited by I. A. Wilson, 10.1006/jmbi.1999.2918
  15. Tulloch Lindsay B., Morgan Hugh P., Hannaert Véronique, Michels Paul A.M., Fothergill-Gilmore Linda A., Walkinshaw Malcolm D., Sulphate Removal Induces a Major Conformational Change in Leishmania mexicana Pyruvate Kinase in the Crystalline State, 10.1016/j.jmb.2008.08.037
  16. Blundell T. Johnson L. (1976) Protein Crystallography, Academic Press, pp. 75–77, Orlando, FL
  17. Potterton Elizabeth, Briggs Peter, Turkenburg Maria, Dodson Eleanor, A graphical user interface to theCCP4 program suite, 10.1107/s0907444903008126
  18. Evans Philip, Scaling and assessment of data quality, 10.1107/s0907444905036693
  19. McCoy Airlie J., Grosse-Kunstleve Ralf W., Adams Paul D., Winn Martyn D., Storoni Laurent C., Read Randy J., Phasercrystallographic software, 10.1107/s0021889807021206
  20. Murshudov G. N., Vagin A. A., Dodson E. J., Refinement of Macromolecular Structures by the Maximum-Likelihood Method, 10.1107/s0907444996012255
  21. Emsley Paul, Cowtan Kevin, Coot: model-building tools for molecular graphics, 10.1107/s0907444904019158
  22. DeLano W. L. (2002) PyMOL v1.2, DeLano Scientific, San Carlos, CA
  23. Christofk Heather R., Vander Heiden Matthew G., Harris Marian H., Ramanathan Arvind, Gerszten Robert E., Wei Ru, Fleming Mark D., Schreiber Stuart L., Cantley Lewis C., The M2 splice isoform of pyruvate kinase is important for cancer metabolism and tumour growth, 10.1038/nature06734
  24. Davis I. W. Leaver-Fay A. Chen V. B. Block J. N. Kapral G. J. Wang X. Murray L. W. Bryan Arendall Iii W. Snoeyink J. Richardson J. S. (2007) Nucleic Acids Res. W375–W83
  25. Dombrauckas Jill D., Santarsiero Bernard D., Mesecar Andrew D., Structural Basis for Tumor Pyruvate Kinase M2 Allosteric Regulation and Catalysis†,‡, 10.1021/bi0474923
  26. Valentini Giovanna, Chiarelli Laurent, Fortin Riccardo, Speranza Maria L., Galizzi Alessandro, Mattevi Andrea, The Allosteric Regulation of Pyruvate Kinase : A SITE-DIRECTED MUTAGENESIS STUDY, 10.1074/jbc.m001870200
  27. Mattevi Andrea, Valentini Giovanna, Rizzi Menico, Speranza M.Luisa, Bolognesi Martino, Coda Alessandro, Crystal structure of Escherichia coli pyruvate kinase type I: molecular basis of the allosteric transition, 10.1016/s0969-2126(01)00207-6
  28. Ericsson Ulrika B., Hallberg B. Martin, DeTitta George T., Dekker Niek, Nordlund Pär, Thermofluor-based high-throughput stability optimization of proteins for structural studies, 10.1016/j.ab.2006.07.027
  29. Changeux J.-P., Allosteric Mechanisms of Signal Transduction, 10.1126/science.1108595
  30. Perutz M. F., Mechanisms of cooperativity and allosteric regulation in proteins, 10.1017/s0033583500003826
  31. Vander Heiden M. G., Cantley L. C., Thompson C. B., Understanding the Warburg Effect: The Metabolic Requirements of Cell Proliferation, 10.1126/science.1160809
  32. Stetak A., Veress R., Ovadi J., Csermely P., Keri G., Ullrich A., Nuclear Translocation of the Tumor Marker Pyruvate Kinase M2 Induces Programmed Cell Death, 10.1158/0008-5472.can-06-2870
  33. Christofk Heather R., Vander Heiden Matthew G., Wu Ning, Asara John M., Cantley Lewis C., Pyruvate kinase M2 is a phosphotyrosine-binding protein, 10.1038/nature06667
  34. Eigenbrodt, Crit. Rev. Oncog., 3, 91 (1992)
  35. Monod Jacque, Wyman Jeffries, Changeux Jean-Pierre, On the nature of allosteric transitions: A plausible model, 10.1016/s0022-2836(65)80285-6
  36. Tsai Chung-Jung, del Sol Antonio, Nussinov Ruth, Allostery: Absence of a Change in Shape Does Not Imply that Allostery Is Not at Play, 10.1016/j.jmb.2008.02.034