Structural basis for the negative allostery between Ca2+- and Mg2+- binding in the intracellular Ca2+-receptor calbindin D(9k)

Protein Science

Volumn 6, Issue 6, 1997, Pages 1139-1147

  Andersson, Maria ^a   Malmendal, Anders ^a   Linse, Sara ^a   Ivarsson, Ianrik ^a   Forsén, Sture ^a   Anders Svensson, L ^a  

^a LUND UNIVERSITY   (Sweden)

Author keywords

Allosteric interaction; Calcium binding protein; Cooperativity; EF hand protein; Magnesium binding; Nuclear magnetic resonance; X ray crystallography

Indexed keywords

CALBINDIN; CALCIUM BINDING PROTEIN; CALCIUM ION; MAGNESIUM ION; METAL ION;

ALLOSTERISM; AMINO TERMINAL SEQUENCE; ARTICLE; CALCIUM BINDING; CARBOXY TERMINAL SEQUENCE; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FAMILY; X RAY CRYSTALLOGRAPHY;

EID: 0030947396     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1002/pro.5560060602     Document Type: Article

References (39)

1. 9k. J Mol Biol 220:173-189.
2. 9k reveal details of the structural changes of step-wise ion binding. J Mol Bol 252:102-121.
3. Black CB, Cowan JA. 1996a. Magnesium-dependent enzymes in nucleic acid biochemistry. In: Cowan JA, ed. The biological chemistry of magnesium. New York: VCH publishers Inc. pp 137-158.
4. Black CB, Cowan JA. 1996b. Magnesium-dependent enzymes in general metabolism. In: Cowan JA. ed. The biological chemistry of magnesium. New York: VCH Publishers Inc. pp 159-183.
5. Brünger AT. 1992. X-PLOR (Version 3.1), A system for X-ray crystallography and NMR. New Haven, Connecticut: Yale University Press.
6. 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Application of an integrated approach to spin system identification in proteins. J Mol Bol 202:603-622.
7. 1H nuclear magnetic resonance spectrum of French bean plastocyanin. Sequential resonance assignments, secondary structure and global fold. J Mol Bol 202:623-636.
8. Christakos S, Gabrielides C, Rhoten WB. 1989. Vitamin D-dependent calcium binding proteins: Chemistry, distribution, functional considerations, and molecular biology. Endocr Rev 10:3-26.
9. Collaborative Computational Project Number 4. 1994. Acta Crystallogr D50:760-763.
10. Declercq JP, Tinant B, Parello J, Rambaud J. 1991. Ionic interactions with parvalbumins: crystal structure determination of pike 4-10 parvalbumin in four different ionic environments. J Mol Bol 220:1017-1039.
11. Drohal AC, Amburgey JC, Abildgaand F, Starlich MR, Baldisseri D, Weber DJ. 1996. Solution structure of rat, apo-5100B (ββ) as determined by NMR spectroscopy. Biochemistry 35:11577-11588.
12. Ebel H, Gunther T. 1980. Magnesium metabolism. J Clin Chem Clin Biochem 18:257-270.
13. Eberhard M, Erne P. 1994. Calcium and magnesium binding to rat parvalbumin. FEBS Lett 222:21-26.
14. Falke JJ, Drake SK, Hazard AL, Peersen OB. 1994. Molecular tuning of ion binding to calcium signalling proteins. Q Rev Biophys 27:219-290.
15. Hemmingsen C, Staun M, Olgaard K. 1996. Effects of magnesium on renal and intestinal calbindin-D. Miner Electrolyte Metab 20:265-273.
16. Hofmann T, Eng S, Lilja H, Drakenberg T, Vogel HJ, Forsen S. 1988. Site-site interactions in EF-hand calcium binding proteins Eur J Biochem 172:307-313.
17. Houdasse H, Cohen C. 1996. Strucure of the regulatory domain of scallop myosin at 2 Å resolution: Implications for regulation. Structure 15:21-32.
18. Johansson C, Brodin P, Grundström T, Thulin E, Forsén S, Drakenberg T. Biophysical studies of engineered mutant proteins based on calbindin D9k modified in the pseudo EF-hand. Eur J Biochem 157:455-460.
19. Jones TA, Zou JY, Cowan SW, Kjeldgaard M. 1991. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr A47:110-119.
20. Kabsch W. 1993. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26:795-800.
21. Kilby PM, Van Eldik LJ, Roberts GCK. 1996. The solution structure of the bovine SlOOB protein dimer in the calcium-free state. Structure 4:1041-1052.
22. 1H NMR studies of the minor (cis-Pro-43) isoform and the Pro43Gly mutant. Biochemistry 29:4400-4409.
23. 9k. J Mol Bol 231:711-734.
24. Kraulis P. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr 24:946-950.
25. Kretsinger RH, Nockolds CE. 1973. Carp muscle calcium binding protein. J Biol Chem 248:3313-3326.
26. Laskowski RA, MacArthur MW, Moss DS, Thornton JM. 1993. PROCHECK: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 26:283-291.
27. 9k. Biochemistry 30:154-162.
28. Nakayama S, Moncrief ND, Kretsinger RH. 1992. Evolution of EF-hand calcium-modulated proteins. II. Domain of several subfamilies have diverse evolutionary histories. J Mol Evol 34:416-448.
29. Persson E, Selander M, Linse S, Drakenberg T, Öhlin AK, Stenflo J. 1989. Calcium binding to the isolated β-hydroxyaspartic acid-containing epidermal growth factor-like domain of bovine factor X. J Biol Chem 264:16897-16904.
30. 2+-binding proteins. Nat Struct Biol 2:790-796.
31. Schäfer BW, Heizmann CW. 1996. The S100 family of EF-hand calcium-binding proteins: Functions and pathology. Trends Biochem Sci 21:134-140.
32. 9k determined by NMR spectroscopy. J Mol Bol 249:441-462.
33. Strynadka NC, James MN. 1989 Crystal structures of the helix-loop-helix calcium-binding proteins. Annu Rev Biochem 55:951-998.
34. 9k observed by X-ray crystallography. J Mol Bol 223:601-606.
35. Szebenyi DM, Moffat K. 1986. The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. J Biol Chem 267:8761-8777.
36. Vogel HJ, Drakenberg T, Forsen S, O'Neil JD, Hofmann T. 1985. Structural differences in the two calcium binding sites of the porcine intestinal calcium binding protein: A multinuclear NMR study. Biochemistry 24:3870-3876.
37. 9k and specific mutants. Biochem Biophys Res Commun 170:603-608.
38. Williams RJP. 1976 Calcium in biological systems, Cambridge, UK: Cambridge University Press.
39. 9k: NMR studies of the N56A mutant. Protein Sci 4:1045-1055.