ATP-induced conformational changes of the nucleotide-binding domain of Na,K-atpase

Nature Structural Biology

Volumn 10, Issue 6, 2003, Pages 468-474

  Hilge, Mark ^a,b   Siegal, Gregg ^a   Vuister, Geerten W ^b   Güntert, Peter ^c   Gloor, Sergio M ^d   Abrahams, Jan Pieter ^a  

^a LEIDEN UNIVERSITY   (Netherlands)

^b RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^c RIKEN YOKOHAMA INSTITUTE   (Japan)

^d UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM); ADENOSINE TRIPHOSPHATE; NUCLEOTIDE; PHOSPHATE; POTASSIUM ION; SODIUM ION; THAPSIGARGIN;

ARTICLE; BINDING AFFINITY; CELL MEMBRANE; CONFORMATIONAL TRANSITION; HYDROLYSIS; ION TRANSPORT; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN STRUCTURE;

ADAPTOR PROTEIN COMPLEX 2; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NA(+)-K(+)-EXCHANGING ATPASE; NUCLEOTIDES; PROTEASE INHIBITORS; PROTEIN CONFORMATION; RATS; SEQUENCE HOMOLOGY, AMINO ACID; THAPSIGARGIN;

EID: 0038442766     PISSN: 10728368     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsb924     Document Type: Article

References (38)

1. Skou, J.C. The influence of some cations on an adenosine triphosphatase from peripheral nerves. Biochim. Biophys. Acta 23, 394-401 (1957).
2. Horisberger, J.D., Lemas, V., Krähenbühl, J.P. & Rossier, B.C. Structure-function relationship of Na,K-ATPase. Annu. Rev. Physiol. 53, 565-584 (1991).
3. 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).
4. Jorgensen, J.R. & Pedersen, P.A. Role of phylogenetically conserved amino acids in folding of Na,K-ATPase. Biochemistry 40, 7301-7308 (2001).
5. Kaplan, J.H. Biochemistry of Na,K-ATPase. Annu. Rev. Biochem. 71, 511-535 (2002).
6. Toyoshima, C., Nakasako, M., Nomura, H. & Ogawa, H. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution. Nature 405, 647-655 (2000).
7. Toyoshima, C. & Nomura, H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611 (2002).
8. Zhang, P., Toyoshima, C., Yonekura, K., Green, N.M. & Stokes, D.L. Structure of the calcium pump from sarcoplasmic reticulum at 8-A resolution. Nature 392, 835-839 (1998).
9. 2+-ATPase. J. Mol. Biol. 316, 201-211 (2002).
10. 2 states. Biophys. J. 80, 2187-2197 (2001).
11. Hebert, H., Purhonen, P., Vorum, H., Thomsen, K. & Maunsbach, A.B. Three-dimensional structure of renal Na,K-ATPase from cryo-electron microscopy of two-dimensional crystals. J. Mol. Biol. 314, 479-494 (2001).
12. +-ATPase in the open conformation. Nature 392, 840-843 (1998).
13. 2+-ATPase of cardiac sarcoplasmic reticulum are critical for functional association with phospholamban. J. Biol. Chem. 269, 22929-22932 (1994).
14. 2+ binding and energy transduction in Na,K-ATPase. Biochim. Biophys. Acta 1505, 57-74 (2001).
15. 2+-ATPase produces pumps defective in ATP binding. J. Biol. Chem. 271, 25778-25789 (1996).
16. Wang, K. & Farley, R.A. Lysine 480 is not an essential residue for ATP-binding or hydrolysis by Na,K-ATPase. J. Biol. Chem. 267, 3577-3580 (1992).
17. 567 for high-affinity binding of ATP, ADP, or MgATP. Biochemistry 41, 1451-1456 (2002).
18. Teramachi, S., Imagawa, T., Kaya, S. & Taniguchi, K. Replacement of several single amino acid side chains exposed to the inside of the ATP-binding pocket induces different extents of affinity change in the high and low affinity ATP-binding sites of rat Na/K-ATPase. J. Biol. Chem. 270, 37394-37400 (2002).
19. +-ATPase. Science 297, 1692-1696 (2002).
20. +-ATPase. J. Biol. Chem. 270, 29971-29975 (1995).
21. Therien, A.G. & Blostein, R. Mechanisms of sodium pump regulation. Am. J. Physiol. Cell Physiol. 279, C541-566 (2000).
22. +-ATPase α-subunit is essential for AP-2 binding and clathrin-dependent endocytosis. J. Biol. Chem. 277, 17108-17111 (2002).
23. 13C labeling. Biochemistry 28, 7510-7516 (1989).
24. Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR6, 277-293 (1995).
25. Bartels, C., Xia, T.H., Billeter, M., Güntert, P. & Wüthrich, K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6, 1-10 (1995).
26. Herrmann, T., Güntert, P. & Wüthrich, K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319, 209-227 (2002).
27. Güntert, P., Mumenthaler, C. & Wüthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298 (1997).
28. Cornell, W.D. et al. A second generation force-field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 117, 5179-5197 (1995).
29. Koradi, R., Billeter, M. & Güntert, P. Point-centered domain decomposition for parallel molecular dynamics simulation. Comput. Phys. Commun. 124, 139-147 (2000).
30. Vriend, G. WHATIF: a molecular modeling and drug design program. J. Mol. Graph. 52, 29-36 (1990).
31. Laskowski, R.A., Rullmann, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486 (1996).
32. Koradi, R., Billeter, M. & Wüthrich, K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55 (1996).
33. Kraulis, P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
34. Nicholls, A., Sharp, K. & Honig, B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296 (1991).
35. Humphrey, W., Dalke, A. & Schulten, K. VMD - visual molecular dynamics. J. Mol. Graph. 14, 33-38 (1996).
36. Wriggers, W., Milligan, R.A. & McCammon, J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125, 185-195 (1999).
37. Kleywegt, G.J. & Jones, T.A. A super position. ESF/CCP4 Newslett. 31, 9-14 (1994).
38. Garrett, D.S., Seok, Y.J., Peterkofsky, A., Clore, G.M. & Gronenborn, A.M. Identification by NMR of the binding surface for the histidine-containing phosphocarrier protein HPr on the N-terminal domain of enzyme I of the Escherichia coli phosphotransferase system. Biochemistry 36, 4393-4398 (1997).