Crystal structure of the Atx1 metallochaperone protein at 1.02 Å resolution

Structure

Volumn 7, Issue 6, 1999, Pages 605-617

  Rosenzweig, Amy C ^a   Huffman, David L ^a   Hou, Melody Y ^a   Wernimont, Amy K ^a   Pufahl, Robert A ^a   O'Halloran, Thomas V ^a  

^a NORTHWESTERN UNIVERSITY   (United States)

Author keywords

Copper transport; Direct methods; Menkes syndrome; Mercury coordination; Shake and Bake

Indexed keywords

CHAPERONE; METALLOPROTEIN;

ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; X RAY ANALYSIS;

EID: 0033153380     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80082-3     Document Type: Article

References (48)

1. Linder, M.C. & Hazegh-Azam, H. (1996). Copper biochemistry and molecular biology. Am. J. Clin. Nutr. 63, 797S-811S.
2. Dancis, A., Haile, D., Yuan, D.S. & Klausner, R.D. (1994). The Saccharomyces cerevisiae copper transport protein (Ctr1p). Biochemical characterization, regulation by copper, and physiologic role in copper uptake. J. Biol. Chem. 269, 25660-25667.
3. Valentine, J.S. & Gralla, EB. (1997). Delivering copper inside yeast and human cells. Science 278, 817-818.
4. Moller, J.V., Juul, B. & Lemaire, M. (1996). Structural organization, ion transport, and energy transduction of P-type ATPases. Biochim. Biophys. Acta 1286, 1-51.
5. Askwith, C., et al., & Kaplan, J. (1994). The FET3 gene of S. Cerevisiae encodes a multicopper oxidase required for ferrous iron uptake. Cell 76, 403-410.
6. Silva, D.M.D., Askwith, C.C., Eide, D. & Kaplan, J. (1995). The FET3 gene product required for high affinity iron transport in yeast is a cell surface ferroxidase. J. Biol. Chem. 270, 1098-1101.
7. Yuan, D.S., Stearman, R., Dancis, A., Dunn, T., Beeler, T. & Klausner, R.D. (1995). The Menkes/Wilson disease gene homologue in yeast provides copper to a ceruloplasmin-like oxidase required for iron uptake. Proc. Natl Acad. Sci. USA 92, 2632-2636.
8. Pufahl, R.A., et al., & O'Halloran, T.V. (1997). Metal ion chaperone function of the soluble Cu(l) receptor, Atx1. Science 278, 853-856.
9. Lin, S.-J. & Culotta, V.C. (1995). The ATX1 gene of Saccharomyces cerevisiae encodes a small metal homeostasis factor that protects cells against reactive oxygen toxicity. Proc. Natl Acad. Sci. USA 92, 3784-3788.
10. Lin, S.-J., Pufahl, R.A., Dancis, A., O'Halloran, T.V. & Culotta, V.C. (1997). A role for the Saccharomyces cerevisiae ATX1 gene in copper trafficking and iron transport. J. Biol. Chem. 272, 9215-9220.
11. Zhou, B. & Gitschier, J. (1997). hCTR1: A human gene for copper uptake identified by complementation in yeast. Proc. Natl Acad. Sci. USA 94, 7481-7486.
12. Klomp, L.W.J., Lin, S.-J., Yuan, D.S., Klausner, R.D., Culotta, V.C. & Gitlin, J.D. (1997). Identification and functional expression of HAH1, a novel human gene involved in copper homeostasis. J. Biol. Chem. 272, 9221-9226.
13. Harris, Z.L., Takahashi, Y., Miyajima, H, Serizawa, M., MacGillivray, R.T. & Gitlin, J.D. (1995). Aceruloplasminemia: Molecular characterization of this disorder of iron metabolism. Proc. Natl Acad. Sci. USA 92, 2539-2543.
14. Bull, P.C., Thomas, G.R., Rommens, J.M., Forbes, J.R. & Cox, D.W. (1993). The Wilson disease gene is a putative copper transporting ATPase similar to the menkes gene. Nat. Genet. 5, 327-337.
15. Vulpe, C., Levinson, B., Whitney, S., Packman, S. & Gitschier, J. (1993). Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper-transporting ATPase. War. Genet. 3, 7-13.
16. Bull, P.C. & Cox, D.W. (1994). Wilson disease and Menkes disease: New handles on heavy-metal transport. Trends Genet. 10, 246-252.
17. Dancis, A., et al., & Klausner, R.D. (1994). Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport. Cell 76, 393-402.
18. Culotta, V.C., Klomp, L.W.J., Strain, J., Casareno, R.L.B., Krems, B. & Gitlin, J.D. (1997). The copper chaperone for superoxide dismutase. J. Biol. Chem. 272, 23469-23472.
19. DiDonato, M., Narindrasorasak, S., Forbes, J.R., Cox, D.W. & Sarkar, B. (1997). Expression, purification, and metal binding properties of the N-terminal domain from the Wilson disease putative copper-Transporting ATPase (ATP7B). J. Biol. Chem. 272, 33279-33282.
20. Lutsenko, S., Petrukhin, K., Cooper, M.J., Gilliam, C.T. & Kaplan, J.H. (1997). N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. J. Biol. Chem. 272, 18939-18944.
21. Hung, I.H., Casareno, R.L.B., Labesse, G., Matthews, F.S. & Gitlin, J.D. (1998). HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense. J. Biol. Chem. 273, 1749-1754.
22. Gitschier, J., Moffat, B., Reilly, D., Wood, W.I. & Fairbrother, W.J. (1998). Solution structure of the fourth metal binding domain from the Menkes copper-transporting ATPase. War. Struct. Biol. 5, 47-54.
23. Steele, R.A. & Opella, S.J. (1997). Structures of the reduced and mercury-bound forms of MerP, the periplasmic protein from the bacterial mercury detoxification system. Biochem. 36, 6885-6895.
24. Qian, H., Sahlman, L., Eriksson, P., Hambraeus, C., Edlund, U. & Sethson, I. (1998). NMR solution structure of the oxidized form of MerP, mercuric ion binding protein involved in bacterial mercuric ion resistance. Biochemistry 37, 9316-9322.
25. Miller, R., Gallo, S.M., Khalak, H.G. & Weeks, C.M. (1994). SnB: Crystal structure determination via shake and bake. J. Appl. Crystallogr. 27, 613-621.
26. Brünger, A.T. (1993). X-PLOR Manual Version 3.1: A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
27. Sheldrick, G.M. & Schneider, T.R. (1997). SHELXL: High-resolution refinement. Method. Enzymol. 277, 319-343.
28. Hubbard, T.J.P., Murzin, A.G., Brenner, S.E. & Chothia, C. (1997). SCOP - A structural classification of proteins database. Nucleic Acids Res, 25, 236-239.
29. Thunnissen, M.M.G.M., Taddei, N., Liguri, G., Ramponi, G. & Nordlund, P. (1997). Crystal structure of a common type acylphosphatase from bovine testis. Structure 5, 69-79.
30. Kissinger, C.R., Sieker, L.C., Adman, E.T. & Jensen, L.H. (1993). Refined crystal structure of ferredoxin II from desulfovibrio gigas at 1.7 Å. J. Mol. Biol. 219, 693-715.
31. Sridhar, V., Prasad, G.S., Burgess, B.K. & Stout, C.D. (1998). Crystal structures of ferricyanide-oxidized [Fe-S] clusters in Azotobacter vinelandii ferredoxin I. J. Biol. Inorg. Chem. 3, 140-149.
32. Tranqui, D. & Jesior, J.C. (1995). Structure of the ferredoxin from clostridium acidurici: Model at 1.8 Å resolution. Acta Crystallogr. D 51, 155-159.
33. Wright, J.W., Natan, M.J., MacDonnell, F.M., Ralston, D.M. & O'Halloran, T.V. (1990). Mercury(II) thiolate chemistry and the mechanism of the heavy metal biosensor MerR. Prog, Inorg. Chem. 38, 323-412.
34. 199Hg NMR. Inorg. Chem. 36, 2926-2927..
35. Watton, S.P., Wright, J.G., MacDonnell, F.M., Bryson, J.W., Sabat, M. & O'Halloran, T.V. (1990). Trigonal mercuric complex of an aliphatic thiolate: A spectroscopic and structural model for the receptor site in the Hg(II) biosensor MerR. J. Am. Chem. Soc. 112, 2824-2826.
36. 199Hg chemical shift as a probe of coordination environments in blue copper proteins. Inorg, Chem. 34, 2497-2498.
37. Utschig, L.M., Bryson, J.W. & O'Halloran, T.V. (1995). Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex. Science 268, 380-385.
38. Stites, W.E. (1997). Protein-protein interactions: Interface structure, binding thermodynamics, and mutational analysis. Chem. Rev. 97, 1233-1250.
39. Bogan, A.A. & Thorn, K.S. (1998). Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9.
40. Deng, H.-X., et al., & Siddique, T. (1993). Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase. Science 261, 1047-1051.
41. Otwinowski, Z. (1993). Oscillation data reduction program. In Proceedings of the CCP4 Study Weekend: Data Collection and Processing. (Sawyer, L., Isaacs, N. & Bailey, S., eds), pp. 56-62, SERC Daresbury Laboratory, Warrington, UK.
42. Collaborative Computational Project, Number 4. (1994). The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763.
43. Blessing, R.H. (1989). DREADD - Data reduction and error analysis for single-crystal diffractometer data. J. Appl. Crystallogr. 22, 396-397.
44. Jones, T.A., Zou, J.-Y., Cowan, S.W. & Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and location of errors in these models. Acta Crystallogr. A 47, 110-119.
45. Laskowski, R.A. (1993). PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
46. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
47. Evans, S.V. (1993). SETOR: Hardware lighted, three-dimensional solid model representations of macromolecules. J. Mol. Graphics 11, 134-138.
48. Nicholls, A., Sharp, K.A. & Honig, B. (1991). Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.