Crystal structure of the calcium pump with a bound ATP analogue

Nature

Volumn 430, Issue 6999, 2004, Pages 529-535

  Toyoshima, Chikashi ^a   Mizutani, Tatsuaki ^a,b  

^a UNIVERSITY OF TOKYO   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CELL MEMBRANES; MUSCLE; PUMPS;

NUCLEOTIDES; SARCOPLASMIC RETICULUM;

CRYSTAL STRUCTURE;

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; CALCIUM ION; MAGNESIUM ION; 5' ADENYLYL (BETA,GAMMA METHYLENE)DIPHOSPHONATE; 5'-ADENYLYL (BETA,GAMMA-METHYLENE)DIPHOSPHONATE; CALCIUM; DRUG DERIVATIVE; MAGNESIUM; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; WATER;

BIOLOGY;

ANIMAL TISSUE; ARTICLE; BINDING SITE; CELL ORGANELLE; CRYSTAL STRUCTURE; CYTOPLASM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; PROTEIN STRUCTURE; SARCOPLASMIC RETICULUM; SKELETAL MUSCLE; STRUCTURE ANALYSIS; ANIMAL; CHEMICAL STRUCTURE; CHEMISTRY; HYDROGEN BOND; METABOLISM; PHOSPHORYLATION; PROTEIN TERTIARY STRUCTURE; RABBIT; X RAY CRYSTALLOGRAPHY;

ANIMALIA;

ADENOSINE TRIPHOSPHATE; ANIMALS; BINDING SITES; CALCIUM; CALCIUM-TRANSPORTING ATPASES; CRYSTALLOGRAPHY, X-RAY; CYTOPLASM; HYDROGEN BONDING; MAGNESIUM; MODELS, MOLECULAR; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; RABBITS; SARCOPLASMIC RETICULUM; SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES; WATER;

EID: 3242888769     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02680     Document Type: Article

References (45)

1. Møller, J. V., Juul, B. & le Maire, M. Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286, 1-51 (1996).
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. Albers, R. W. Biochemical aspects of active transport. Annu. Rev. Biochem. 36, 727-756 (1967).
4. 2+-dependent ATPase of the sarcoplasmic reticulum. Annu. Rev. Biochem. 48, 275-292 (1979).
5. 2+ transport by the sarcoplasmic reticulum ATPase. Biochim. Biophys. Acta 1318, 52-70 (1997).
6. 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).
7. Toyoshima, C. & Nomura, H. Structural changes in the calcium pump accompanying the dissociation of calcium. Nature 418, 605-611 (2002).
8. 2+-ATPase. J. Mol. Biol. 316, 201-211 (2002).
9. 2+-ATPases. J. Biol. Chem. 272, 28815-28818 (1997).
10. 2+-dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence. Nature 316, 696-700 (1985).
11. 2+ ATPase of sarcoplasmic reticulum. Expression in developing skeletal muscle. J. Biol. Chem. 262, 3768-3774 (1987).
12. 2+ transport ATPase by thapsigargin at subnanomolar concentrations. J. Biol. Chem. 266, 13503-13506 (1991).
13. 2+-ATPase of sarcoplasmic reticulum. FEBS Lett. 555, 106-110 (2003).
14. Brünger, A. T. Extension of molecular replacement; a new search strategy based on Patterson correlation refinement. Acta Crystallogr. A 46, 46-57 (1990).
15. 1ATP states: a limited proteolysis study. FEBS Lett. 505, 129-135 (2001).
16. 2+ binding properties after removal of cytoplasmic fragments by proteinase K? J. Biol. Chem. 270, 20123-20134 (1995).
17. 2+ATPase (SERCA). J. Biol. Chem. 278, 28938-28943 (2003).
18. 2+ at different sites. J. Biol. Chem. 269, 15931-15936 (1994).
19. 2+ transport (SERCA) ATPase. Biochemistry 39, 8758-8767 (2000).
20. Orlowski, S. & Champeil, P. Kinetics of calcium dissociation from its high-affinity transport sites on sarcoplasmic reticulum ATPase. Biochemistry 30, 352-361 (1991).
21. 2+-ATPase affects cation binding from both sides of the membrane and destabilizes the occluded enzyme forms. Biochemistry 37, 10961-10971 (1998).
22. 2+-ATPase phosphoenzyme intermediate. J. Biol. Chem. (in the press).
23. 2+ occlusion and phosphoenzyme processing. J. Biol. Chem. 279, 15888-15896 (2004).
24. Bilwes, A. M., Quezada, C. M., Croal, L. R., Crane, B. R. & Simon, M. I. Nucleotide binding by the histidine kinase CheA. Nature Struct. Biol. 8, 353-360 (2001).
25. Hilge, M. et al. ATP-induced conformational changes of the nucleotide-binding domain of Na,K-ATPase. Nature Struct. Biol. 10, 468-474 (2003).
26. 2+-ATPase produces pumps defective in ATP binding. J. Biol. Chem. 271, 25778-25789 (1996).
27. Cappello, V., Tramontano, A. & Koch, U. Classification of proteins based on the properties of the ligand-binding site: the case of adenine-binding proteins. Proteins 47, 106-115 (2002).
28. 2+-ATPase and its substrate ATP with infrared spectroscopy. J. Biol. Chem. 278, 10112-10118 (2003).
29. 2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 265, 22223-22227 (1990).
30. 2+-ATPase of sarcoplasmic reticulum. J. Biol. Chem. 264, 13038-13042 (1989).
31. 2+-ATPase. J. Biol. Chem. 274, 25227-25236 (1999).
32. 2+-ATPase for MgATP binding and subsequent catalytic steps. Plasticity of the nucleotide-binding site. J. Biol. Chem. 278, 20245-20258 (2003).
33. Jacobsen, M. D., Pedersen, P. A. & Jorgensen, P. L. Importance of Na,K-ATPase residue α1-Arg544 in the segment Arg544-Asp567 for high-affinity binding of ATP, ADP, or MgATP. Biochemistry 41, 1451-1456 (2002).
34. McIntosh, D. B. The ATP binding sites of P-type ion transport ATPases. Adv. Mol. Cell Biol. 23A, 33-99 (1998).
35. Aravind, L., Galperin, M. Y. & Koonin, E. V. The catalytic domain of the P-type ATPase has the haloacid dehalogenase fold. Trends Biochem. Sci. 23, 127-129 (1998).
36. Wang, W. et al. Structural characterization of the reaction pathway in phosphoserine phosphatase: crystallographic 'snapshots' of intermediate states. J. Mol. Biol. 319, 421-431 (2002).
37. Lahiri, S. D., Zhang, G., Dunaway-Mariano, D. & Allen, K. N. Caught in the act: the structure of phosphorylated β-phosphoglucomutase from Lactococcus lactis. Biochemistry 41, 8351-8359 (2002).
38. Eletr, S. & Inesi, G. Phospholipid orientation in sarcoplasmic membranes: spin-label ESR and proton MNR studies. Biochim. Biophys. Acta 282, 174-179 (1972).
39. Coll, R. J. & Murphy, A. J. Purification of the CaATPase of sarcoplasmic reticulum by affinity chromatography. J. Biol. Chem. 259, 14249-14254 (1984).
40. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-325 (1997).
41. Brünger, A. T. et al. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
42. Collaborative Computational Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
43. Kabsch, W. & Sander, C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637 (1983).
44. Kraulis, P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).
45. Hayward, S. Structural principles governing domain motions in proteins. Proteins 36, 425-435 (1999).