Hostname: page-component-848d4c4894-8bljj Total loading time: 0 Render date: 2024-07-01T19:00:55.765Z Has data issue: false hasContentIssue false
  • English
  • Français

New crystal form of β-lactoglobulin

Published online by Cambridge University Press:  01 June 2009

Thales L. Rocha ,
Sharon Brownlow ,
Keith N. Saddler ,
Linda A. Fothergill-Gilmore  and
Lindsay Sawyer
Thales L. Rocha
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Sharon Brownlow
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Keith N. Saddler
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Linda A. Fothergill-Gilmore
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Lindsay Sawyer
Affiliation:
Department of Biochemistry, University of Edinburgh, George Square, Edinburgh EH8 9XD, UK
Get access Rights & Permissions [Opens in a new window]

Summary

The milk whey protein β-lactoglobulin has been isolated from ovine milk, purified and crystallized in a form suitable for X-ray crystallography. The crystals, which diffract to 1·9 Å resolution, belong to the trigonal space group P3121 with unit cell lengths a = b = 99·8 Å, c = 67·7 Å and unique angle γ = 120·0°. Although there have been many crystal forms reported for bovine β-lactoglobulin, none has been reported with these unit cell parameters. A preliminary native data set has been collected and a molecular replacement solution obtained, using the structure of dimeric bovine β-lactoglobulin as the search model. The importance of the ovine structure in relation to that of the bovine is discussed.

Type
Original Articles
Information
Journal of Dairy Research , Volume 63 , Issue 4 , November 1996 , pp. 575 - 584
Copyright
Copyright © Proprietors of Journal of Dairy Research 1996

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Armstrong, J. McD., McKenzie, H. A. & Sawyer, W. H. 1967 On the fractionation of β-lactoglobulin and α-lactalbumin. Biochimica et Biophysica Ada 147 60–72CrossRefGoogle ScholarPubMed
Aschaffenburg, R. & Drewry, J. 1957 Improved method for the preparation of crystalline β-lactoglobulin and α-lactalbumin from cow's milk. Biochemical Journal 65 273–277CrossRefGoogle ScholarPubMed
Aschaffenburg, R., Green, D. W. & Simmons, R. M. 1965 Crystal forms of β-lactoglobulin. Journal of Molecular Biology 13 194–201CrossRefGoogle ScholarPubMed
Batt, C. A., Rabson, L. D., Wong, D. W. S. & Kinsella, J. E. 1990 Expression of recombinant bovine β-lactoglobulin in Escherichia coli. Agricultural and Biological Chemistry 54 949–955Google ScholarPubMed
Bell, K. & McKenzie, H. A. 1967 The whey proteins of ovine milk: β-lactoglobulins A and B. Biochimica et Biophysica Ada 147 123–134CrossRefGoogle ScholarPubMed
CCP4 (Collaborative Computational Project NO. 4) 1994 The CCP4 suite: programs for protein crystallography. Ada Crystallographica D50 760–763Google Scholar
Clark, A. J., Simons, P., Wilmut, I. & Lathe, R. 1987 Pharmaceuticals from transgenic livestock. Trends in Biotechnology 5 20–24CrossRefGoogle Scholar
Diaz de Villegas, M. C., Oria, R., Sala, F. J. & Calvo, M. 1987 Lipid binding by β-lactoglobulin of cow milk. Milchwissenschaft 42 357–358Google Scholar
Erhardt, G., Godovac-Zimmermann, J. & Conti, A. 1989 Isolation and complete primary sequence of a new ovine wild-type β-lactoglobulin C. Biological Chemistry Hoppe-Seyler 370 757–762CrossRefGoogle ScholarPubMed
Flower, D. R. 1994 The lipocalin protein family-a role in cell regulation (minireview). FEBS Letters 354 7–11CrossRefGoogle Scholar
Gaye, P., Hue-Delahaie, D., Mercier, J.-C., Soulier, S., Vilotte, J. -L. & Furet, J. -P. 1986 Ovine β-lactoglobulin messenger RNA: nucleotide sequence and mRNA levels during functional differentiation of the mammary gland. Biochimie 68 1097–1107CrossRefGoogle ScholarPubMed
Green, D. W., Aschaffenburg, R., Camerman, A., Coppola, J. C., Dunnill, P., Simmons, R. M., Komorowski, E. S., Sawyer, L., Turner, E. M. C. & Woods, K. F. 1979 Structure of bovine β-laetoglobulin at 6 A resolution. Journal of Molecular Biology 131 375–397CrossRefGoogle Scholar
Green, D. W., North, A. C. T. & Aschaffenburg, R. 1956 Crystallography of the β-lactoglobulins of cows' milk. Biochimica et Biophysica Ada 21 583–585CrossRefGoogle Scholar
Hambling, S. G., McAlpine, A. S. & Sawyer, L. 1992 β-Lactoglobulin. In Advanced Dairy Chemistry—1. Proteins, pp. 140–191 (Ed. Fox, P. F.). London: Elsevier Applied ScienceGoogle Scholar
Hampel, A., Labanauskas, M., Connors, P. G., Kirkegard, L., Rajbhandary, U. L., Sigler, P. B. & Bock, R. M. 1968 Single crystals of transfer RNA from formylmethionine and phenylalanine transfer RNA's. Science 162 1384–1387CrossRefGoogle ScholarPubMed
Jakob, E. & Puhan, Z. 1992 Technological properties of milk as influenced by genetic polymorphism of milk proteins – a review. International Dairy Journal 2 157–178CrossRefGoogle Scholar
Kabsch, W. 1988 Evaluation of single-crystal X-ray diffraction data from a position-sensitive detector. Journal of Applied Crystallography 21 916–924CrossRefGoogle Scholar
Kraulis, P. J. 1991 MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. Journal of Applied Crystallography 24 946–950CrossRefGoogle Scholar
Laemmli, U. K. 1970 Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 680–685CrossRefGoogle ScholarPubMed
McAlpine, A. S. & Sawyer, L. 1990 β-Lactoglobulin: a protein drug carrier ? Biochemical Society Transactions 18 879CrossRefGoogle ScholarPubMed
Monaco, H. L., Zanotti, G., Spadon, P., Boloonesi, M., Sawyer, L. & Eliopoulos, E. E. 1987 Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2·5 Å resolution. Journal of Molecular Biology 197 695–706CrossRefGoogle ScholarPubMed
Moneret-Vautrin, A., Humbert, G., Alais, C. & Grilliat, J. P. 1982 [Recent studies on immunoallergic properties of milk proteins] Lait 62 396–408CrossRefGoogle Scholar
Navaza, J. 1994 AMoRe: an automated package for molecular replacement. Ada Crystallographica A50 157–163Google Scholar
Papiz, M. Z., Sawyer, L., Eliopoulos, E. E., North, A. C. T., Findlay, J. B. C., Sivaprasadarao, R., Jones, T. A., Newcomer, M. E. & Kraulis, P. J. 1986 The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324 383–385CrossRefGoogle ScholarPubMed
Pervaiz, S. & Brew, K. 1985 Homology of β-lactoglobulin, serum retinol-binding protein, and protein HC. Science 228 335–337CrossRefGoogle ScholarPubMed
Rocha, T. L., Paterson, G., Crimmins, K., Boyd, A., Sawyer, L. & Fothergill-Gilmore, L. A. 1996 Expression and secretion of recombinant ovine β-lactoglobulin in Saccharomyces cerevisiae and Kluyveromyces lactis. Biochemical Journal 313 927–932CrossRefGoogle ScholarPubMed
Roefs, S. P. F. M. & De Kruif, K. G. 1994 A model for the denaturation and aggregation of β-lactoglobulin. European Journal of Biochemistry 226 883–889CrossRefGoogle Scholar
Sedmak, J. J. & Grossberg, S. E. 1977 A rapid, sensitive, and versatile assay for protein using Coomassie brilliant blue G250. Analytical Biochemistry 79 544–552CrossRefGoogle ScholarPubMed
Silva, M. C., Wong, D. W. S. & Batt, C. A. 1990 Cloning and partial nucleotide sequence of the genomic bovine β-lactoglobulin gene. Nucleic Acids Research 18 3051CrossRefGoogle ScholarPubMed
Zhang, X. -J., Wozniak, J. A. & Matthews, B. W. 1995 Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozyme. Journal of Molecular Biology 250 527–552CrossRefGoogle ScholarPubMed