Crystal structure of the sodium-potassium pump at 2.4 resolution

Nature

Volumn 459, Issue 7245, 2009, Pages 446-450

  Shinoda, Takehiro ^a   Ogawa, Haruo ^a   Cornelius, Flemming ^b   Toyoshima, Chikashi ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b AARHUS UNIVERSITY   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); FXYD PROTEIN; KIDNEY ENZYME; PHOSPHATE; POTASSIUM ION; PROTON; REGULATOR PROTEIN; UNCLASSIFIED DRUG; WATER;

CONCENTRATION (COMPOSITION); CRYSTAL STRUCTURE; CYTOPLASM; ENZYME; MOLECULAR ANALYSIS; WATER;

ALPHA CHAIN; ARTICLE; BETA CHAIN; BINDING AFFINITY; BINDING SITE; CRYSTAL STRUCTURE; ENZYME PHOSPHORYLATION; EXPERIMENTAL PIG; ION TRANSPORT; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; RECTUM GLAND; SEQUENCE HOMOLOGY; SHARK;

ANIMALS; BINDING SITES; CALCIUM-TRANSPORTING ATPASES; CRYSTALLOGRAPHY, X-RAY; FLUORIDES; HUMANS; MAGNESIUM COMPOUNDS; MEMBRANE PROTEINS; MODELS, MOLECULAR; PHOSPHOPROTEINS; PHOSPHORYLATION; POTASSIUM; PROTEIN CONFORMATION; PROTEIN SUBUNITS; SALT GLAND; SHARKS; SODIUM-POTASSIUM-EXCHANGING ATPASE; SWINE;

ANIMALIA; CHONDRICHTHYES; SUIDAE;

EID: 66249147196     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature07939     Document Type: Article

References (30)

1. Albers, R. W. Biochemical aspects of active transport. Annu. Rev. Biochem. 36, 727-756 (1967).
2. Post, R. L., Hegyvary, C. & Kume, S. Activation by adenosine triphosphate in the phosphorylation kinetics of sodium and potassium ion transport adenosine triphosphatase. J. Biol. Chem. 247, 6530-6540 (1972).
3. Mahmmoud, Y. A., Vorum, H. & Cornelius, F. Identification of a phospholemman-like protein from shark rectal glands. Evidence for indirect regulation of Na,K-ATPase by protein kinase c via a novel member of the FXYDY family. J. Biol. Chem. 275, 35969-35977 (2000).
4. Garty, H. & Karlish, S. J. Role of FXYD proteins in ion transport. Annu. Rev. Physiol. 68, 431-459 (2006).
5. Morth, J. P. et al. Crystal structure of the sodium-potassium pump. Nature 450, 1043-1049 (2007).
6. Lutsenko, S. & Kaplan, J. H. An essential role for the extracellular domain of the Na,K-ATPase β-subunit in cation occlusion. Biochemistry 32, 6737-6743 (1993).
7. Hasler, U., Crambert, G., Horisberger, J. D. & Geering, K. Structural and functional features of the transmembrane domain of the Na,K-ATPase b subunit revealed by tryptophan scanning. J. Biol. Chem. 276, 16356-16364 (2001).
8. Geering, K. The functional role of β subunits in oligomeric P-type ATPases. J. Bioenerg. Biomembr. 33, 425-438 (2001).
9. + -ATPase. J. Biol. Chem. 283, 27982-27990 (2008).
10. Toyoshima, C., Nomura, H. & Tsuda, T. Lumenal gating mechanism revealed in calcium pump crystal structures with phosphate analogues. Nature 432, 361-368 (2004).
11. Toyoshima, C., Nakasako, M., Nomura, H. & Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405,647-655 (2000).
12. Jacobsen, M. D., Pedersen, P. A. & Jorgensen, P. L. Importance of Na,K-ATPase residue alpha 1-Arg544 in the segment Arg544-Asp567 for high-affinity binding of ATP, ADP, or MgATP. Biochemistry 41, 1451-1456 (2002).
13. Toyoshima, C. & Mizutani, T. Crystal structure of the calcium pump with a bound ATP analogue. Nature 430, 529-535 (2004).
14. Sørensen, T. L., Møller, J. V. & Nissen, P. Phosphoryl transfer and calcium ion occlusion in the calcium pump. Science 304, 1672-1675 (2004).
15. 2+-ATPase for MgATP binding and subsequent catalytic steps. Plasticity of the nucleotide-binding site. J. Biol. Chem. 278, 20245-20258 (2003).
16. Murphy, A. J. & Hoover, J. C. Inhibition of the Na,K-ATPase by fluoride. Parallels with its inhibition of the sarcoplasmic reticulum CaATPase. J. Biol. Chem. 267, 16995-17000 (1992).
17. Jensen, A. M., Sørensen, T. L., Olesen, C., Møller, J. V. & Nissen, P. Modulatory and catalytic modes of ATP binding by the calcium pump. EMBO J. 25, 2305-2314 (2006).
18. Toyoshima, C. & Nomura, H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611 (2002).
19. Brown, I. D. & Wu, K. K. Empirical parameters for calculating cation-oxygen bond valences. Acta Crystallogr. B 32, 1957-1959 (1976).
20. Jewell-Motz, E. A. & Lingrel, J. B. Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains. Biochemistry 32, 13523-13530 (1993).
21. Nielsen, J. M., Pedersen, P. A., Karlish, S. J. & Jorgensen, P. L. Importance of intramembrane carboxylic acids for occlusion of K1 ions at equilibrium in renal Na,K-ATPase. Biochemistry 37, 1961-1968 (1998).
22. 2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms. Biochemistry 37, 10961-10971 (1998).
23. +-ATPase. Proc. Natl Acad. Sci. USA 99, 15977-15982 (2002).
24. Ueno, T. & Sekine, T. Study on calcium transport by sarcoplasmic reticulum vesicles using fluorescence probes. J. Biochem.84, 787-794 (1978).
25. Pietrobon, D. Familial hemiplegic migraine. Neurotherapeutics 4, 274-284 (2007).
26. + -ATPase α3 gene ATP1A3 are associated with rapid-onset dystonia parkinsonism. Neuron 43, 169-175 (2004).
27. Cornelius, F., Turner, N. & Christensen, H. R. Modulation of Na,K-ATPase by phospholipids and cholesterol. II. Steady-state and presteady-state kinetics. Biochemistry 42, 8541-8549 (2003).
28. +-ATPase activity by cholesterol: role of hydration. Biochemistry 39, 10928-10935 (2000).
29. Colonna, T. E., Huynh, L. & Fambrough, D. M. Subunit interactions in the Na,K-ATPase explored with the yeast two-hybrid system. J. Biol. Chem. 272, 12366-12372 (1997).
30. 2+ ATPase. Proc. Natl Acad. Sci. USA 100, 467-472 (2003).