Crystal structures of RIα subunit of cyclic adenosine 5′-monophosphate (cAMP)-dependent protein kinase complexed with (R p)-adenosine 3′,5′-cyclic monophosphothioate and (S p)-adenosine 3′,5′-cyclic monophosphothioate, the phosphothioate analogues of cAMP

Biochemistry

Volumn 43, Issue 21, 2004, Pages 6620-6629

  Wu, Jian ^a   Jones, John M ^a   Xuong, Nguyen Huu ^a   Ten Eyck, Lynn F ^a,b   Taylor, Susan S ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; DIMERIZATION; DIMERS; ENZYMES; MUTAGENESIS; SOLVENTS;

MUTANTS; PHOSPHATE BINDING CASSETTE (PBC);

BIOCHEMISTRY;

ADENOSINE 3',5' CYCLIC MONOPHOSPHOTHIOATE; ARGININE; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DERIVATIVE; DIMER; LIGAND; PHOSPHATE BINDING PROTEIN; SOLVENT; UNCLASSIFIED DRUG; ADENOSINE 3',5' PHOSPHOROTHIOATE; ADENOSINE-3',5'-CYCLIC PHOSPHOROTHIOATE; CYCLIC AMP; DRUG DERIVATIVE; NUCLEOTIDE; REGULATORY SUBUNIT RIALPHA, CYCLIC AMP DEPENDENT PROTEIN KINASE; REGULATORY SUBUNIT RIALPHA, CYCLIC-AMP-DEPENDENT PROTEIN KINASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; BINDING SITE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DELETION MUTANT; DIMERIZATION; ENZYME ACTIVATION; ENZYME SUBUNIT; LIGAND BINDING; MOLECULAR DYNAMICS; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; SIGNAL TRANSDUCTION; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE; CHEMICAL STRUCTURE; CHEMISTRY; METABOLISM; PROTEIN TERTIARY STRUCTURE; STEREOISOMERISM; X RAY CRYSTALLOGRAPHY;

VERTEBRATA;

BINDING SITES; CRYSTALLOGRAPHY, X-RAY; CYCLIC AMP; CYCLIC AMP-DEPENDENT PROTEIN KINASES; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; STEREOISOMERISM; THIONUCLEOTIDES;

EID: 2542523982     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0302503     Document Type: Article

References (36)

1. Mitra, S., Zubay, G., and Landy, A. (1975) Evidence for the preferential binding of the catabolite gene activator protein (CAP) to DNA containing the lac promoter. Biochem. Biophys. Res. Commun. 67, 857-863.
2. Walsh, D. A., Perkins, J. P., and Krebs, E. G. (1968) An adenosine 3′,5′-monophosphate-dependent protein kinase from rabbit skeletal muscle. J. Biol. Chem. 243, 3763-3765.
3. Taylor, S. S., Buechler, J. A., and Yonemoto, W. (1990) cAMP-dependent protein kinase: framework for a diverse family of regulatory enzymes. Annu. Rev. Biochem. 59, 971-1005.
4. Ludwig, J., Margalit, T., Eismann, E., Lancet, D., and Kaupp, U. B. (1990) Primary structure of cAMP-gated channel from bovine olfactory epithelium. FEBS Lett. 270, 24-29.
5. de Rooij, J., Zwartkruis, F. J., Verheijen, M. H., Cool, R. H., Nijman, S. M., Wittinghofer, A., and Bos, J. L. (1998) Epac is a Rapl guanine-nucleotide-exchange factor directly activated by cyclic AMP. Nature 396, 474-477.
6. Kawasaki, H., Springett, G. M., Mochizuki, N., Toki, S., Nakaya, M., Matsuda, M., Housman, D. E., and Graybiel, A. M. (1992) A family of cAMP-binding proteins that directly activate Rap1. Science 282, 2275-2279.
7. Døskeland, S. O., Maronde, E., and Gjertsen, B. T. (1993) The genetic subtypes of cAMP-dependent protein kinase - Functionally different or redundant? Biochim. Biophys. Acta 1178, 249-258.
8. Francis, S. H., and Corbin, J. D. (1999) Cyclic nucleotide-dependent protein kinases: intracellular receptors for cAMP and cGMP action. Crit. Rev. Clin. Lab. Sci. 36, 275-328.
9. Scott, J. D. (1991) Cyclic nucleotide-dependent protein kinases. Pharmacol. Ther. 50, 123-145.
10. Titani, K., Sasagawa, T., Ericsson, L. H., Kumar, S., Smith, S. B., Krebs, E. G., and Walsh, K. A. (1984) Amino acid sequence of the regulatory subunit of bovine type I adenosine cyclic 3′,5′-phosphate dependent protein kinase. Biochemistry 23, 4193-4199.
11. Øgreid, D., Ekanger, R., Suva, R. H., Miller, J. P., and Døskeland, S. O. (1989) Comparison of the two classes of binding sites (A and B) of type I and type II cyclic-AMP-dependent protein kinases by using cyclic nucleotide analogs. Eur. J. Biochem. 181, 19-31.
12. Rannels, S. R., and Corbin, J. D. (1981) Studies on the function of the two intrachain cAMP binding sites of protein kinase. J. Biol. Chem. 256, 7871-7876.
13. Døskeland, S. O., Øgreid, D., Ekanger, R., Sturm, P. A., Miller, J. P., and Suva, R. H. (1983) Mapping of the two intrachain cyclic nucleotide binding sites of adenosine cyclic 3′,5′-phosphate dependent protein kinase I. Biochemistry 22, 1094-1101.
14. Ringheim, G. E., Saraswat, L. D., Bubis, J., and Taylor, S. S. (1988) Deletion of cAMP-binding site B in the regulatory subunit of cAMP-dependent protein kinase alters the photoaffinity labeling of site A. J. Biol. Chem. 263, 18247-18252.
15. Neitzel, J. J., Dostmann, W. R. G., and Taylor, S. S. (1991) Role of MgATP in the activation and reassociation of cAMP-dependent protein kinase I: consequences of replacing the essential arginine in cAMP binding site A. Biochemistry 30, 733-739.
16. Herberg, F. W., Taylor, S. S., and Dostmann, W. R. G. (1996) Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase. Biochemistry 35, 2934-2942.
17. Zorn, M., Fladmark, K., Øgreid, D., Jastorff, B., Døskeland, S. O., and Dostmann, W. R. G. (1995) Ala335 is essential for high-affinity cAMP-binding of both sites A and B of cAMP-dependent protein kinase type I. FEBS Lett 362, 291-294.
18. Øgreid, D., and Døskeland, S. O. (1982) Activation of protein kinase isoenzymes under near physiological conditions. Evidence that both types (A and B) of cAMP binding sites are involved in the activation of protein kinase by cAMP and 8-N3-cAMP. FEBS Lett 150, 161-166.
19. Bubis, J., and Taylor, S. S. (1987) Correlation of photolabeling with occupancy of cAMP binding sites in the regulatory subunit of cAMP-dependent protein kinase I. Biochemistry 26, 3478-3486.
20. Su, Y., Dostmann, W. R. G., Herberg, F. W., Durick, K., Xuong, N., Eyck, L. T., Taylor, S. S., and Varughese, K. L. (1995) Regulatory subunit of protein kinase A: structure of deletion mutant with cAMP binding domains. Science 269, 807-813.
21. Diller, T. C., Madhusudan, Xuong, N., and Taylor, S. S. (2001) Molecular basis for regulatory subunit diversity in cAMP-dependent protein kinase: crystal structure of the type II beta regulatory subunit. Structure 9, 73-82.
22. Kang, G., Joseph, J. W., Chepumy, O. G., Monaco, M., Wheeler, M. B., Bos, J. L., Schwede, F., Genieser, H. G., and Holz, G. G. (2003) Epac-selective cAMP analog 8-pCPT-2′-O-Me-cAMP as a stimulus for Ca2+-induced Ca2+ release and exocytosis in pancreatic beta-cells. J. Biol. Chem. 278, 8279-8285.
23. Schwede, F., Maronde, E., Genieser, H. G., and Jastorff, B. (2000) Cyclic nucleotide analogs as biochemical tools and prospective drugs. Pharmacol. Ther. 87, 199-226.
24. Rothermel, J. D., and Botelho, L. H. P. (1988) A mechanistic and kinetic analysis of the interactions of the diastereoisomers of adenosine 3′,5′-(cyclic)phosphorothioate with purified cyclic AMP-dependent protein kinase. Biochem. J. 251, 757-762.
25. DeWit, R. J. W., Hekstra, D., Jastorff, B., Stec, W. J., Baraniak, J., Driel, R. V., and van Haastert, P. J. M. (1984) Inhibitory action of certain cyclophosphate derivatives of cAMP on cAMP-dependent protein kinases. Eur. J. Biochem. 152, 255-260.
26. Dostmann, W. R. G., Taylor, S. S., Genieser, H. G., Jastorff, B., Døskeland, S. O., and Øgreid, D. (1990) Probing the cyclic nucleotide binding sites of cAMP-dependent protein kinases I and II with analogs of adenosine 3′,5′-cyclic phosphorothioates. J. Biol. Chem. 265, 10484-10491.
27. Dostmann, W. R. G. (1995) (RP)-cAMPS inhibits the cAMP-dependent protein kinase by blocking the cAMP-induced conformational transition. FEBS Lett. 375, 231-234.
28. Dostmann, W. R. G., and Taylor, S. S. (1991) Identifying the molecular switches that determine whether (Rp)-cAMPS functions as an antagonist or an agonist in the activation of cAMP-dependent protein kinase I. Biochemistry 30, 8710-8716.
29. Saraswat, L. D., Filutowics, M., and Taylor, S. S. (1988) Expression and mutagenesis of the regulatory subunit of cAMP-dependent protein kinase in Escherichia coli. Method Enzymol. 159, 325-336.
30. Otwinowski, Z., and Minor, W. (1997) Processing of X-ray data collected in oscillation mode. Method Enzymol. 276, 307-326.
31. Brunger, A. T., Adams, P. D., and Clore, G. M. (1998) Crystallography and NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D54, 905-921.
32. Roussel, A., and Cambillau, C. (1991) Turbo-Frodo, Silicon Graphics partner geometry dictionary, Silicon Graphics Inc., Mountain View, CA.
33. Morris, A. L., MacArthur, M. W., Hutchinson, E. G., and Thornton, J. M. (1992) Stereochemical quality of protein structure coordinates. Proteins: Struct., Funct., Genet. 12, 345-364.
34. Weber, I. T., and Steitz, T. A. (1987) Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5 Å resolution. J. Mol. Biol. 198, 311-326.
35. Wu, J., Brown, S., Xuong, N. H., Taylor, S. S. RIα subunit of PKA: A cAMP-free structure reveals a hydrophobic capping mechanism for docking cAMP into site B. Structure, in press.
36. Anand, G. S., Hughes, C. A., Jones, J. M., Taylor, S. S., and Komives, E. A. (2002) Amide H/2H exchange reveals communication between the cAMP and catalytic subunit-binding sites in the R(I)alpha subunit of protein kinase A. J. Mol Biol. 323, 377-386.