Peptide folding, metal-binding mechanisms, and binding site structures in metallothioneins

Experimental Biology and Medicine

Volumn 231, Issue 9, 2006, Pages 1488-1499

  Duncan, Kelly E Rigby ^a   Ngu, Thanh T ^a   Chan, Jayna ^a   Salgado, Maria T ^a   Merrifield, Maureen E ^a   Stillman, Martin J ^a  

^a UNIVERSITY OF WESTERN ONTARIO   (Canada)

Author keywords

Cd(II), Zn(II), Cu(I), As(III); Emission spectroscopy; EXAFS; Fucus vesiculosus; Kinetic analysis; Metal domain; MM MD; Protein folding; XANES

Indexed keywords

ARSENIC; CADMIUM; COPPER; METALLOTHIONEIN;

ABSORPTION SPECTROPHOTOMETRY; BINDING SITE; CIRCULAR DICHROISM; CONFERENCE PAPER; ELECTROSPRAY MASS SPECTROMETRY; KINETICS; METAL BINDING; NONHUMAN; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE; STOICHIOMETRY; ULTRAVIOLET SPECTROSCOPY;

ALGAE; FUCUS VESICULOSUS;

EID: 33749602354     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: 10.1177/153537020623100907     Document Type: Conference Paper

References (50)

1. Kagi JHR, Nordberg M, Eds. Metallothionein I. Basel: Birkhauser Verlag, 1979.
2. Kagi JHR, Kojima Y, Eds. Metallothionein II. Basel: Birkhauser Verlag, 1987.
3. Klaassen CD, Ed. Metallothionein IV. Basel: Birkhauser Verlag, 1997.
4. Suzuki KT, Imura N, Kimura M, Eds. Metallothionein III. Basel: Birkhauser Verlag, 1993.
5. Riordan JF, Vallee BL. Methods in Enzymology. San Diego: Academic Press, Vol 205:p681, 1991.
6. Stillman MJ, Shaw III CF, Suzuki KT. Metallothioneins: synthesis, structure and properties of metallothioneins, phytochelatins and metalthiolate complexes. New York: VCH Publishers, Inc., 1992.
7. Stillman MJ. Metallothioneins. Coord Chem Rev 144:461-511, 1995.
8. Miles AT, Hawksworth GM, Beattie JH, Rodilla V. Induction, regulation, degradation, and biological significance of mammalian metallothioneins. Crit Rev Biochem Mol Biol 35:35-70, 2000.
9. Yang Y, Maret W, Vallee BL. Differential fluorescence labelling of cysteinyl clusters uncovers high tissue levels of thionein. Proc Natl Acad Sci U S A 98:5556-5559, 2001.
10. Bagla P. Arsenic-laced well water poisoning Bangladesh. National Geographic News. Available at: http://news.nationalgeographic.com/news/2003/06/ 0605_030605_arsenicwater.html. Accessed August 2006.
11. Hug S, Wegelin M, Gechter D, Canonica L. Arsenic contamination of ground water: disastrous consequences in Bangladesh. EAWAG News 49:18-20, 2000.
12. Demel S, Shi J, Martin P, Rosen BP. Arginine 60 in the ArsC arsenate reductase of E. coli plasmid R773 determines the chemical nature of the bound As(III) product. Protein Sci 13:2330-2340, 2004.
13. Leach AR. Molecular modelling: principles and applications. Harlow, England: Prentice Hall, p720, 2001.
14. Schlick T. Molecular modeling and simulation: an interdisciplinary guide. New York: Springer-Verlag, p634, 2002.
15. Morris CA, Nicolaus B, Sampson V, Harwood JL, Kille P. Identification and characterization of a recombinant metallothionein protein from a marine alga, Fucus vesiculosus. Biochem J 338:553-560, 1999.
16. Robbins AH, McRee DE, Williamson M, Collett SA, Xuong NH, Furey WF, Wang BC, Stout CD. Refined crystal structure of cadmium-zinc metallothionein at 2.0 Å resolution. J Mol Biol 221:1269-1293, 1991.
17. 7]metallothionein-2a in aqueous solution determined by nuclear magnetic resonance. J Mol Biol 201:637-657, 1988.
18. Otvos JD, Armitage IM. Structure of the metal clusters in rabbit liver metallothionein. Proc Natl Acad Sci U S A 77:7094-7098, 1980.
19. Shapiro SG, Squibb KS, Markowitz LA, Cousins RJ. Cell-free synthesis of metallothionein directed by rat liver polyadenylated messenger ribonucleic acid. Biochem J 175:833-840, 1978.
20. Enescu M, Renault J-P, Pommeret S, Mialocq J-C, Pin S. Ab initio study of Cd-thiol complexes: application to the modelling of the metallothionein active site. Phys Chem Chem Phys 5:3762-3767, 2003.
21. Chang C-C, Huang PC. Semi-empirical simulation of Zn/Cd binding site preference in the metal binding domains of mammalian metallothionein. Protein Eng 9:1165-1172, 1996.
22. Berweger CD, Theil W, van Gunsteren WF. Molecular-dynamics simulation of the beta domain of metallothionein with a semi-empirical treatment of the metal core. Proteins 41:299-315, 2000.
23. Fowle DA, Stillman MJ. Comparison of the structures of the metalthiolate binding site in Zn(II)-, Cd(II)-, and Hg(II)-metallothioneins using molecular modeling techniques. J Biomol Struct Dyn 14:393-406, 1997.
24. Presta A, Fowle DA, Stillman MJ. Structural model of rabbit liver copper metallothionein. J Chem Soc Dalton Trans 6:977-984, 1997.
25. Rigby KE, Stillman MJ. Structural studies of metal-free metallothionein. Biochem Biophys Res Comm 325:1271-1278, 2004.
26. Rigby KE, Stillman MJ. Molecular dynamics study on the folding and metallation of the individual domains of metallothionein. Proteins 62:159-172, 2006.
27. Petering DH, Fowler BA. Roles of metallothionein and related proteins in metal metabolism and toxicity: problems and perspectives. Environ Health Perspect 65:217-224, 1986.
28. Aggett PJ, Barclay SM. Neonatal trace element metabolism. In: Cowett RM, Ed. Principles of Perinatal-Neonatal Metabolism. New York: Springer-Verlag, pp500-530, 1991.
29. Green AR, Presta A, Gasyna Z, Stillman MJ. Luminescence probe of copper-thiolate cluster formation within mammalian metallothionein. Inorg Chem 33:4159-4168, 1994.
30. Nielson KB, Winge DR. Order of metal binding in metallothionein. J Biol Chem 258:13063-13069, 1983.
31. Nielson KB, Winge DR. Preferential binding of copper to the beta domain of metallothionein. J Biol Chem 259:4941-4946, 1984.
32. Salgado MT, Stillman MJ. Cu(I) distribution in metallothionein fragments. Biochem Biophys Res Comm 318:73-80, 2004.
33. Briggs RW, Armitage IM. Evidence for site-selective metal binding in calf liver metallothionein. J Biol Chem 257:1259-1262, 1982.
34. Bremner I, Young BW. Isolation of (copper, zinc)-thioneins from the livers of copper-injected rats. Biochem J 157:517-520, 1976.
35. Bremner I, Young BW. Isolation of (copper, zinc-) thioneins from pig liver. Biochem J 155:631-635, 1976.
36. Jiang G, Gong Z, Li X-F, Cullen WR, Le XC. Interaction of trivalent arsenicals with metallothionein. Chem Res Toxicol 16:873-880, 2003.
37. Toyama M, Yamashita M, Hirayama N, Murooka Y. Interactions of arsenic with human metallothionein-2. J Biochem (Tokyo) 132:217-221, 2002.
38. Brunner H, Nuber B, Poll L, Roidl G, Wachter J. Novel inorganic cage structures based on AsS ligands and cyclopentadienylruthenium groups. Chem-Eur J 3:57-61, 1997.
39. 3-. Observation of unique thioarsenate ligands and Pt-As bonds. Inorg Chem 33:5372-5373, 1994.
40. Ngu TT, Stillman MJ. The kinetics of arsenic binding to metallothionein. J Am Chem Soc 128 (39) (in press), 2006.
41. Chan J, Merrifield ME, Soldatov AV, Stillman MJ. XAFS spectral analysis of the cadmium coordination geometry in cadmium thiolate clusters in metallothionein. Inorg Chem 44:4923-4933, 2005.
42. Ankudinov AL, Ravel B, Rehr JJ, Conradson SD. Real-space multiple-scattering calculation and interpretation of x-ray-absorption near-edge structure. Phys Rev B 58:7565-7576, 1998.
43. Ankudinov AL, Bouldin CE, Rehr JJ, Sims J, Hung H. Parallel calculation of electron multiple scattering using Lanczos algorithms. Phys Rev B 65:104-107, 2002.
44. Pickering IJ, Prince RC, George GN, Rauser WE, Wickramasinghe WA, Watson AA, Dameron CT, Dance IG, Fairlie DP, Salt DE. X-ray absorption spectroscopy of cadmium phytochelatin and model systems. Biochim Biophys Acta 1429:351-364, 1999.
45. Newville M, Carroll S, O'Day P, Waychunas G. The XAFS Model Compound Library. Available at: http://cars9.uchicago.edu/∼newville/ModelLib/. Accessed August 2004.
46. 18-MT formed from rabbit liver metallothionein-2. J Am Chem Soc 116:11004-11013, 1994.
47. Kagi JHR, Vallee BL. Metallothionein: a cadmium and zinc-containing protein from equine renal cortex. II. Physicochemical properties. J Biol Chem 236:2435-2442, 1961.
48. Kagi JHR, Vallee BL. Metallothionein: a cadmium- and zinc-containing protein from equine renal cortex. J Biol Chem 235:3460-3465, 1960.
49. Kojima Y, Berger C, Vallee BL, Kagi JHR. Amino-acid sequence of equine renal metallothionein-1B. Proc Natl Acad Sci U S A 73:3413-3417, 1976.
50. Calderone V, Dolderer B, Hartmann HJ, Echner H, Luchinat C, Bianco CD, Mangani S, Weser U. The crystal structure of yeast copper thionein: the solution of a long-lasting enigma. Proc Natl Acad Sci U S A 102:51-56, 2005.