Phe475 and Glu446 but not Ser445 participate in ATP-binding to the α-subunit of Na+/K+-ATPase

Biochemical and Biophysical Research Communications

Volumn 297, Issue 1, 2002, Pages 154-159

  Kubala, Martin ^a,b   Hofbauerová, Kateřina ^a,b   Ettrich, Rüdiger ^a,b,c   Kopecký Jr , Vladimír ^a,b   Krumscheid, Rita ^d   Plášek, Jaromír ^b   Teisinger, Jan ^a   Schoner, Wilhelm ^d   Amler, Evžen ^a  

^a INSTITUTE OF PHYSIOLOGY   (Czech Republic)

^b CHARLES UNIVERSITY   (Czech Republic)

^c UNIVERSITY OF SOUTH BOHEMIA   (Czech Republic)

^d JUSTUS LIEBIG UNIVERSITY   (Germany)

Author keywords

ATP binding site; Fluorescence spectroscopy; Na+ K+ ATPase; TNP ATP

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ALANINE; GLUTAMINE; GLYCINE; PHENYLALANINE; SERINE; TRYPTOPHAN;

ARTICLE; BINDING SITE; CYTOPLASM; FLUORESCENCE; PRIORITY JOURNAL; PROTEIN BINDING; SITE DIRECTED MUTAGENESIS;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; FLUORESCENT DYES; GLUTAMIC ACID; MICE; MODELS, MOLECULAR; NA(+)-K(+)-EXCHANGING ATPASE; PHENYLALANINE; PROTEIN CONFORMATION; PROTEIN SUBUNITS; RECOMBINANT FUSION PROTEINS; SERINE;

EID: 0036385819     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02089-2     Document Type: Article

References (19)

1. (+)-ATPase, J. Biol. Chem. 269 (1994) 19659-19662.
2. C. Toyoshima, M. Nakasako, H. Nomura, H. Ogawa, Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution, Nature 405 (2000) 647-655.
3. +-ATPase deduced by restraint-based comparative modeling shows only one ATP-binding site, J. Mol. Model. 7 (2001) 184-192.
4. +-ATPase, Biopolymers 67 (2002) 242-246.
5. (+)-ATPase after photochemical labeling with 8-azido-ATP, Biochemistry 33 (1994) 4140-4147.
6. G. Scheiner-Bobis, S. Schreiber, Glutamic acid 472 and lysine 480 of the sodium pump α1 subunit are essential for activity. Their conservation in pyrophosphatases suggests their involvement in recognition of ATP phosphates, Biochemistry 38 (1999) 9198-9208.
7. +-ATPase, FEBS Lett. 441 (1998) 103-105.
8. M.D. Jacobsen, P.A. Pedersen, P.L. Jorgensen, Importance of NaK-ATPase residue α1-Arg544 in the segment Arg544-Asp567 for high-affinity binding of ATP, ADP, or MgATP, Biochemistry 41 (2002) 1451-1456.
9. (+)-ATPase, Biochim. Biophys. Acta 1469 (2000) 133-157.
10. C. Gatto, A.X. Wang, J.H. Kaplan, The M4M5 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 (1998) 10578-10585.
11. C.M. Tran, R.A. Farley, Catalytic activity of an isolated domain of Na,K-ATPase expressed in Escherichia coli, Biophys. J. 77 (1999) 258-266.
12. D.B. Smith, K.S. Johnson, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase, Gene 67 (1988) 31-37.
13. O. Ennis, R. Maytum, T. Mantle, Cloning and overexpression of rat kidney biliverdin IX α reductase as a fusion protein with glutathione S-transferase: stereochemistry of NADH oxidation and evidence that the presence of the glutathione S-transferase domain does not effect BVR-A activity, Biochem. J. 328 (1997) 33-36.
14. T. Hiratsuka, Fluorescence properties of 2′ (or 3′)-O-(2,4,6-trinitrophenyl) adenosine 5′-triphosphate and its use in the study of binding to heavy meromyosin ATPase, Biochim. Biophys. Acta 453 (1976) 293-297.
15. E.G. Moczydlowski, P.A.G. Fortes, Characterization of 2′,3′-O-(2,4,6-trinitrocyclohexadienylidine) adenosine 5′-triphosphate as a fluorescent probe of the ATP site of sodium and potassium transport adenosine triphosphatase. Determination of nucleotide binding stoichiometry and ion-induced changes in affinity for ATP, J. Biol. Chem. 256 (1981) 2346-2356.
16. M. Prokop, J. Damborsky, J. Koca, TRITON: in silico construction of protein mutants and prediction of their activities, Bioinformatics 16 (2000) 845-846.
17. (+)-ATPase, J. Biol. Chem. 268 (1993) 21895-21900.
18. 2+ binding phosphorylation and energy transduction in Na,K-ATPase, J. Biol. Chem. 275 (2000) 37588-37595.
19. G.M. Morris, D. Goodsell, R. Huey, A.J.J. Olson, Distributed automated docking of flexible ligands to proteins: parallel applications of AutoDock 2.4., Comput. Aided Mol. Des. 10 (1996) 293-304.