The phosphatase activity of the isolated H4-H5 loop of Na+/K+ ATPase resides outside its ATP binding site

European Journal of Biochemistry

Volumn 271, Issue 19, 2004, Pages 3923-3936

  Krumscheid, Rita ^a   Ettrich, Rüdiger ^b   Sovová, Zofie ^b   Sušánková, Klára ^c   Lánský, Zdeněk ^c   Hofbauerová, Kateřina ^c,d   Linnertz, Holger ^a   Teisinger, Jan ^c   Amler, Evžen ^c   Schoner, Wilhelm ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b INSTITUTE OF LANDSCAPE ECOLOGY   (Czech Republic)

^c INSTITUTE OF MICROBIOLOGY   (Czech Republic)

^d INSTITUTE OF PHYSIOLOGY   (Czech Republic)

Author keywords

ATPase; H4 H5 loop; P nitrophenylphosphate; Protein expression; TNP ATP

Indexed keywords

2',3' O (TRINITROPHENYL)ADENOSINE 5' TRIPHOSPHATE; 4 NITROPHENYL PHOSPHATE; ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; AMINO ACID; FLUORESCEIN ISOTHIOCYANATE; PHOSPHATASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT;

4-NITROPHENYLPHOSPHATASE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CYTOPLASM; ENZYME STABILITY; EOSINE YELLOWISH-(YS); FLUORESCENT DYES; GLUTATHIONE TRANSFERASE; KIDNEY; MICE; MOLECULAR SEQUENCE DATA; MUTATION; NA(+)-K(+)-EXCHANGING ATPASE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN-TYROSINE-PHOSPHATASE; RECOMBINANT FUSION PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP; SUBSTRATE SPECIFICITY; SWINE;

VERTEBRATA;

EID: 5044236894     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04330.x     Document Type: Article

References (63)

1. Kaplan, J.H. (2002) Biochemistry of Na,K-ATPase. Ann. Rev. Biochem. 71, 511-535.
2. +-ATPase. J. Biol. Chem. 269, 19659-19662.
3. Jorgensen, P.L., Hakansson, K.O. & Karlish, S.J.D. (2003) Structure and mechanism of Na,K-ATPase: Functional Sites and Their Interactions. Ann. Rev. Physiol. 65, 817-849.
4. Schoner, W. (2002) Endogenous cardiac glycosides, a new class of steroid hormones. Eur. J. Biochem. 269, 2440-2448.
5. +-ATPase as a signal transducer. Eur. J. Biochem. 269, 2434-2439.
6. +-ATPase? Eur. J. Biochem. 191, 397-404.
7. +-ATPase and reveal the interaction of two ATP sites during catalysis. J. Biol. Chem. 272, 16315-16321.
8. +-ATPase. Analysis of structural requirements of fluorescent ATP derivatives with a Koshland-Nemethy-Filmer model of two interacting ATP sites. J. Biol. Chem. 274, 1971-1978.
9. +)-dependent ATPase of cell membranes. Biochim. Biophys. Acta 118, 116-123.
10. +)-ATPase. Biochim. Biophys. Acta 241, 57-67.
11. 32P from p-nitrophenylphosphate into a microsomal phosphatase. Mol. Pharmacol. 6, 99-107.
12. +-transport ATPase. J. Biochem. (Tokyo) 129, 335-342.
13. Karlish, S.J.D. (1980) Characterization of conformational changes in (Na,K)-ATPase labeled with fluorescein at the active site. J. Bioenerget. Biomembr. 12, 111-136.
14. 2ATP site. Eur. J. Biochem. 232, 420-424.
15. 1ATP site. Eur. J. Biochem. 253, 245-250.
16. +-ATPase. FEBS Lett. 441, 103-105.
17. +-activated phosphatase reside on different alpha-subunits. J. Biol. Chem. 273, 28813-28821.
18. +-ATPase. In Na/K-ATPase and Related ATPases (Taniguchi, K. & Kaya, S., eds), pp. 349-356. Elsevier Science, Amsterdam.
19. Toyoshima, C., Nakasako, M., Nomura, H. & Ogawa, H. (2000) Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Angström resolution. Nature 405, 647-655.
20. +-ATPase deduced by restraint-based comparative modeling shows only one ATP-binding site. J. Molec. Model. 7, 184-192.
21. Hakansson, K.O. (2003) The Crystallographic Structure of Na, K-ATPase N-domain at 2.6 Å Resolution. J. Mol. Biol. 332, 1175-1182.
22. Hilge, M., Siegal, G., Vuister, G.W., Güntert, P., Gloor, S.M. & Abrahams, J.P. (2003) ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPAse. Nature Struct. Biol. 10, 468-474.
23. +-ATPase. Biochemistry 43, 8303-8311.
24. 2 partial reactions by sequential block of high and low affinity nucleotide sites. J. Biol. Chem. 273, 14277-14284.
25. 32P]ADP) as a photoactivatable probe. Label incorporation before and after blocking the high affinity ATP site with fluorescein isothiocyanate. J. Biol. Chem. 273, 33759-33765.
26. +-transporting ATPase: Location of the 5′-(p-fluorosulfonyl) benzoyaladenosine binding site and soluble peptides release by trypsin. Proc. Natl Acad. Sci. USA 83, 2071-2075.
27. +-ATPase revealed Asp-710 in the catalytic site. FEBS Lett. 217, 111-116.
28. Toyoshima, C. & Nomura, H. (2002) Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611.
29. 2+-ATPase. J. Mol. Biol. 316, 201-211.
30. +)-ATPase: pertinence of the adenine and fluorescein binding sites. Biochim. Biophys. Acta 953, 26-36.
31. Schuurmans Stekhoven, F. & Bonting, S.L. (1981) Transport Adensone Triphosphatses: Properties and Function. Physiol. Rev. 61, 1-76.
32. Schoner, W., Thönges, D., Hamer, E., Antolovic, R., Buxbaum, E., Willeke, M., Serpersu, E.H. & Scheiner-Bobis, G. (1994) Is the sodium pump a functional dimer? In The Sodium Pump (Bamberg, E. & Schoner, W., eds), pp. 332-341. Springer Verlag, New York.
33. +)-activated ATPase preparation. Biochem. Biophys. Res. Commun. 42, 880-885.
34. 5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein. J. Biol. Chem. 273, 10578-10585.
35. 5 cytoplasmic loop of Na,K-ATPase overexpressed in Escherichia coli retains its ability to bind ATP. FEBS Lett. 426, 297-300.
36. Tran, C.M. & Farley, R.A. (1999) Catalytic actvivity of an isolated domain of Na,K-ATPase expressed in Escherichia coli. Biophys. J. 77, 258-266.
37. +)-ATPase. 3. Purification from the outer medulla of mammalian kidney after selective removal of membrane components by sodium dodecyl sulphate. Biochim. Biophys. Acta 356, 36-52.
38. +-activated ATPase from ox brain. Eur. J. Biochem. 1, 334-343.
39. Lowry, O.H., Rosebrough, N.J., Farr, A.L. & Randall, R.J. (1951) Protein measurement with the Folin phenol reagent. J. Biol. Chem. 293, 235-275.
40. Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
41. +-ATPase. Biochemistry 42, 6446-6452.
42. Moczydlowski, E.G. & Fortes, P.A.G. (1981) Characterization of 2′,3′-O-(2,4,6-trinitrocyclohexadieneylidine) adenosine 5′-triphosphate as a fluorescent probe of the ATP site of sodium and potassium adenosine triphosphatse. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP. J. Biol. Chem. 256, 2346-2356.
43. +-ATPase. Methods Enzymol. 156, 278-281.
44. 5 loop of Na/K-ATPase. Eur. Biophys. J. 32, 363-369.
45. Sali, A. & Blundell, T.L. (1993) Comparative protein modeling by satisfaction of spatial restraints. J. Mol. Biol. 234, 779-815.
46. Laskowski, R.A., McArthur, M.W., Moss, D.S. & Thornton, J.M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
47. 2 subunit of the membrane-spanning Na,K-ATPase protein. Acta Cryst. D59, 1259-1261.
48. Thompson, J.D., Gibson, T.J., Plewniak, F., Jeanmougin, F. & Higgins, D.G. (1997) The Clustal-Windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25, 4876-4882.
49. Wang, S., Taberno, L., Zhang, M., Harms, E., Van Etten, R.L. & Staufacher, C.V. (2000) Crystal structure of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cervisiae and its complex with the substrate p-nitrophenyl phosphate. Biochemistry 39, 1903-1914.
50. Morris, G.M., Goodsell, D., Huey, R. & Olson, A.J. (1996) Distributed automated docking of flexible ligands to proteins: Parallel applications of AutoDock 2.4. J. Comp. Aided Mol. Design 10, 293-304.
51. +-ATPase with 4-azido-2-nitrophenyl phosphate. Biochemistry 35, 47-55.
52. Amler, E., Abbott, A. & Ball, W.J.J. (1992) Structural dynamics and oligomeric interactions of Na,K-ATPase monitored using fluorescence energy transfer. Biophys. J. 61, 553-568.
53. +)-ATPase. Biochim. Biophys. Acta 727, 101-107.
54. + on conformational states in membrane-bound renal Na,K-ATPase. Biochemistry 33, 8558-8565.
55. Costa, C.J., Ghatto, C. & Kaplan, J.H. (2003) Interactions between Na,K-ATPase α-subunit ATP binding domains. J. Biol. Chem. 278, 9176-9184.
56. +-ATPase. Biochem. Biophys. Res. Commun. 306, 416-420.
57. +-dependent 3-O-methylfluorescein phosphatase and its use for the assay of enzyme samples with low activities. Anal. Biochem. 66, 265-271.
58. Cavieres, J.D., Lilley, K.S. & Ward, D.G. (2000) Dissecting and mapping two nucleotide binding sites in Na,K-ATPase. In Na/K-ATPase and Related ATPases (Taniguchi, K. & Kaya, S., eds), pp. 115-122. Elsevier Science, Amsterdam.
59. +-ATPase rigid. Eur. J. Biochem. 251, 522-527.
60. +)-ATPase. Biochim. Biophys. Acta 429, 1006-1019.
61. 2+ binding, phosphorylation, and energy transduction in Na,K-ATPase. J. Biol. Chem. 275, 37588-37595.
62. +-ATPase. Biopolymers 67, 242-246.
63. Scheiner-Bobis, G., Mertens, W., Willeke, M. & Schoner, W. (1992) Synthesis and biochemical characterization of the new sulfhydryl-reactive ATP analogue 8-thiocyano-ATP. Its interaction with Na,K-ATPase and kinases. Biochemistry 31, 2107-2113.