Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1

Biochemistry

Volumn 43, Issue 41, 2004, Pages 13046-13053

  Anastassopoulou, Ioanna ^a   Banci, Lucia ^b   Bertini, Ivano ^b   Cantini, Francesca ^b   Katsari, Efthalia ^b   Rosato, Antonio ^b  

^a INSTITUTE OF NANOSCIENCE AND NANOTECHNOLOGY   (Greece)

^b UNIVERSITY OF FLORENCE   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DERIVATIVES; ESCHERICHIA COLI; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; STRUCTURE (COMPOSITION); X RAY CRYSTALLOGRAPHY;

HEAVY ATOMS; HUMAN METALLOCHAPERONE; ROOT-MEAN-SQUARE-DEVIATION (RMSD);

COPPER;

APOPROTEIN; CHAPERONE; COPPER; MONOMER; PROTEIN HAH1; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DATA ANALYSIS; ESCHERICHIA COLI; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; REACTION ANALYSIS; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

ESCHERICHIA COLI;

EID: 5444259690     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0487591     Document Type: Article

References (48)

1. Linder, M. C. (1991) Biochemistry of Copper, Plenum Press, New York.
2. Vulpe, C. D., and Packman, S. (1995) Cellular copper transport, Annu. Rev. Nutr. 15, 293-322.
3. O'Halloran, T. V., and Culotta, V. C. (2000) Metallochaperones: An Intracellular Shuttle Service for Metal Ions, J. Biol. Chem. 275, 25057-25060.
4. Harrison, M.D., Jones, C. E., Solioz, M., and Dameron, C. T. (2000) Intracellular copper routing: the role of copper chaperones, Trends Biochem. Sci. 25 (1), 29-32.
5. Puig, S., and Thiele, D. J. (2002) Molecular mechanisms of copper uptake and distribution, Curr. Opin. Chem. Biol. 6 (2), 171-180.
6. Huffman, D. L., and O'Halloran, T. V. (2000) Energetics of Copper Trafficking Between the Atx1 Metallochaperone and the Intracellular Copper-transporter, Ccc2, J. Biol. Chem. 275, 18611-18614.
7. Rae, T., Schmidt, P. J., Pufahl, R. A, Culotta, V. C., and O'Halloran. T. V. (1999) Undetectable intracellular free copper: the requirement of a copper chaperone for superoxide dismutase, Science 284, 805-808.
8. Rosenzweig, A. C. (2001) Copper delivery by metallochaperone proteins, Acc. Chem. Res. 34 (2), 119-128.
9. Banci, L., and Rosato, A. (2003) Structural genomics of proteins involved in copper homeostasis, Acc. Chem. Res. 36, 215-221.
10. Klomp, L. W., Lin, S. J., Yuan, D., Klausner, R. D., Culotta, V. C, and Gitlin, J. D. (1997) Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis, J. Biol. Chem. 272, 9221-9226.
11. Pufahl, R. A., Singer, C. P., Peariso, K. L., et al. (1997) Metal ion chaperone function of the soluble Cu(I) receptor Atx1, Science 278, 853-856.
12. Petris, M. J., Mercer, J. F., Culvenor, J. G., Lockhart, P., and Camakaris, J. (1996) Ligand-regulated transport of the Menkes copper P-type ATPase efflux pump from the Golgi apparatus to the plasma membrane: a novel mechanism of regulated trafficking, EMBO J. 15, 6084-6095.
13. Amesano, F., Banci, L., and Bertini, I., et al. (2002) Metallochaperones and metal transporting ATPases: a comparative analysis of sequences and structures, Genome Res. 12, 255-271.
14. Walker, J. M., Huster, D., Ralle, M., Morgan, C. T., Blackburn, N. J., and Lutsenko, S. (2004) The N-terminal metal-binding site 2 of the Wilson's disease protein plays a key role in the transfer of copper from Atox1, J. Biol. Chem. 279, 15376-15384.
15. Jones, C. E., Daly, N. L., Cobine, P. A., Craik, D. J., and Dameron, C. T. (2003) Structure and metal binding studies of the second copper binding domain of the Menkes ATPase, J. Struct. Biol. 143 (3), 209-218.
16. Banci, L., Bertini, I., Del Conte, R., D'Onofrio, M., Rosato, A. (2004) Solution structure and backbone dynamics of the Cu(I) and apo-forms of the second metal-binding domain of the Menkes protein ATP7A, Biochemistry 43, 3396-3403.
17. Strausak, D., Howie, M. K., Firth, S. D., et al. (2003) Kinetic analysis of the interaction of the copper chaperone Atox1 with the metal binding sites of the Menkes protein, J. Biol. Chem. 278 (23), 20821-20827.
18. Wernimont, A. K., Yatsunyk, L. A., and Rosenzweig, A. C. (2004) Binding of copper(I) by the Wilson disease protein and its copper chaperone, J. Biol. Chem. 279 (13), 12269-12276.
19. Amesano, F., Banci, L., Bertini, I., and Bonvin, A. M. J. J. (2004) A docking approach to the study of copper trafficking proteins: interaction between metallochaperones and soluble domains of copper ATPases, Structure 12, 669-676.
20. Amesano, F., Banci, L., and Bertini, I., et al. (2001) Characterization of the binding interface between the copper chaperone Atx1 and the first cytosolic domain of Ccc2 ATPase, J. Biol. Chem. 276 (44), 41365-41376.
21. Wernimont, A. K., Huffman, D. L., Lamb, A. L., O'Halloran, T. V., and Rosenzweig, A. C. (2000) Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins, Nat. Struct. Biol. 7 (9), 766-771.
22. Eccles, C., Güntert, P., Billeter, M., and Wüthrich, K. (1991) Efficient analysis of protein 2D NMR spectra using the software package EASY, J. Biomol. NMR 1, 111-130.
23. Güntert, P., Braun, W., and Wüthrich, K. (1991) Efficient computation of three-dimensional protein structures in solution from Nuclear Magnetic Resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA, J. Mol. Biol. 217, 517-530.
24. 15N Enriched Proteins, J. Am. Chem. Soc. 115, 7772-7777.
25. Gagne', R. R, Tsuda, S, Li, M. X., Chandra, M., Smillie, L. B, and Sykes, B. D. (1994) Quantification of the calcium-induced secondary structural changes in the regulatory domain of troponin-C, Protein Sci. 3, 1961-1974.
26. 13C chemical shift data, J. Biomol. NMR 4, 171-180.
27. G̈ntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion Angle Dynamics for NMR Structure Calculation with the new program DYANA, J. Mol. Biol. 275, 283-298.
28. Herrmann, T., Güntert, P., and Wüthrich, K. (2002) Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA, J. Mol. Biol. 319 (1), 209-227.
29. Banci, L., Bertini, I., Ciofi-Baffoni, S., Huffman, D. L., and O'Halloran, T. V. (2001) Solution structure of the yeast copper transporter domain Ccc2a in the apo and Cu(I)-loaded states, J. Biol. Chem. 276 (11), 8415-8426.
30. Case, D. A., Pearlman, D. A., Caldwell, J. W., et al. (1999) AMBER 6, University of California, San Francisco.
31. Banci, L., Benedetto, M., Bertini, I., Del Conte, R., Piccioli, M., and Viezzoli, M. S. (1998) Solution structure of reduced monomeric Q133M2 Copper, Zinc Superoxide Dismutase. Why is SOD a dimeric enzyme? Biochemistry 37, 11780-11791.
32. Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
33. Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-486.
34. 2 values in proteins, J. Magn. Reson. 97, 359-375.
35. Grzesiek, S., and Bax, A. (1993) The importance of not saturating H2O in protein NMR. Application to sensitivity enhancement and NOE measurements, J. Am. Chem. Soc. 115, 12593-12594.
36. Marquardt, D. W. (1963) An algorithm for least-squares estimation of nonlinear parameters, J. Soc. Ind. Appl. Math. 11, 431-441.
37. Mandel, M. A., Akke, M., and Palmer, A. G., III (1995) Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme, J. Mol. Biol. 246, 144-163.
38. Cavanagh, J., Fairbrother, W. J., Palmer, A. G., III, and Skelton, N. J. (1996) Protein NMR Spectroscopy. Principles and practice, Academic Press, San Diego.
39. Grzesiek, S., Bax, A., and Clore, G. M., et al. (1996) The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase, Nat. Struct. Biol. 3 (4), 340-345.
40. Rosenzweig, A. C., Huffman, D. L., Hou, M. Y., Wernimont, A. K., Pufahl, R. A., and O'Halloran, T. V. (1999) Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution, Struct. Fold Des. 7, 605-617.
41. Ralle, M., Lutsenko, S., and Blackburn, N. J. (2003) X-ray absorption spectroscopy of the copper chaperone HAH1 reveals a linear two-coordinate Cu(I) center capable of adduct formation with exogenous thiols and phosphines, J. Biol. Chem. 278 (25), 23163-23170.
42. Arnesano, F., Banci, L., Bertini, I., Huffman, D. L., and O'Halloran, T. V. (2001) Solution Structure of the Cu(I) and Apo forms of the Yeast Metallochaperone, Atx1, Biochemistry 40 (6), 1528-1539.
43. Banci, L., Bertini, I., and Del Conte, R. (2003) The solution structure of apo CopZ from Bacillus subtilis: a further analysis of the changes associated with the presence of copper, Biochemistry 42 (46), 13422-13428.
44. Gitschier, J., Moffat, B., Reilly, D., Wood, W. I., and Fairbrother, W. J. (1998) Solution structure of the fourth metal-binding domain from the Menkes copper-transporting ATPase, Nat. Struct. Biol. 5, 47-54.
45. Banci, L., Bertini, I., Del Conte, R., Mangani, S., and Meyer-Klaucke, W. (2003) X-ray absorption spectroscopy study of CopZ, a copper chaperone in Bacillus subtilis. The coordination properties of the copper ion, Biochemistry 8, 2467-2474.
46. Urvoas, A., Moutiez, M., Estienne, C., Couprie, J., Mintz, E., and Le Clainche, L. (2004) Metal-binding stoichiometry and selectivity of the copper chaperone CopZ from Enterococcus hirae, Eur. J. Biochem. 271 (5), 993-1003.
47. Laskowski, R. A., MacArthur, M. W., and Thornton, J. M. (1998) Validation of protein models derived from experiment, Curr. Opin. Struct. Biol. 8, 631-639.
48. Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: a program for display and analysis of macromolecular structure. J. Mol. Graphics 14, 51-55.