Altered domain closure and iron binding in transferrins: The crystal structure of the Asp60Ser mutant of the amino-terminal half-molecule of human lactoferrin

Journal of Molecular Biology

Volumn 256, Issue 2, 1996, Pages 352-363

  Faber, H Rick ^a   Bland, Tony ^a   Day, Catherine L ^a,b   Norris, Gillian E ^a   Tweedie, John W ^a   Baker, Edward N ^a  

^a MASSEY UNIVERSITY   (New Zealand)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Crystal structure; Domain closure; Iron binding; Lactoferrin; Mutagenesis

Indexed keywords

IRON; IRON BINDING PROTEIN; LACTOFERRIN; MUTANT PROTEIN; TRANSFERRIN; WATER;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; HYDROGEN BOND; IRON BINDING CAPACITY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; STRUCTURE ACTIVITY RELATION;

EID: 0029867181     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0091     Document Type: Article

References (52)

1. Anderson, B. F., Baker, H. M., Dodson, E. J., Norris, G. E., Rumball, S. V., Waters, J. M. & Baker, E. N. (1987). Structure of human lactoferrin at 3.2 Åresolution. Proc. Natl Acad. Sci. USA, 84, 1769-1773.
2. Anderson, B. F., Baker, H. M., Norris, G. E., Rice, D. W. & Baker, E. N. (1989). Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209, 711-734.
3. Anderson, B. F., Baker, H. M., Norris, G. E., Rumball, S. V. & Baker, E. N. (1990). Apolactoferrin structure demonstrates ligand-induced conformational change in transferrins. Nature, 344, 784-787.
4. Bailey, S., Evans, R. W., Garratt, R. C., Gorinsky, B., Hasnain, S., Horsburgh, C., Jhoti, H., Lindley, P. F., Mydin, A., Sarra, R. & Watson, J. L. (1988). Molecular structure of serum transferrin at 3.3 Å resolution. Biochemistry, 27, 5804-5812.
5. Baker, E. N. (1994). Structure and reactivity of transferrins. Advan. Inorg. Chem. 41, 389-463.
6. Baker, E. N. & Hubbard, R. E. (1984). Hydrogen bonding in globular proteins. Prog. Biophys. Mol. Biol. 44, 97-179.
7. Baker, E. N. & Lindley, P. F. (1992). New perspectives on the structure and function of transferrins. J. Inorg. Biochem. 47, 147-160.
8. Baker, E. N., Rumball, S. V. & Anderson, B. F. (1987). Transferrins: insights into structure and function from studies on lactoferrin. Trends Biochem. Sci. 12, 350-353.
9. Baker, E. N., Anderson, B. F., Baker, H. M., Haridas, M., Jameson, G. B., Norris, G. E., Rumball, S. V. & Smith, C. A. (1991). Structure, function and flexibility of human lactoferrin. Int. J. Biol. Macromol. 13, 122-129.
10. Baker, E. N., Baker, H. M., Smith, C. A., Stebbins, M. R., Kahn, M., Hellstrōm, K. E. & Hellström, I. (1992). Human melanotransferrin (p97) has only one functional iron-binding site. FEBS Letters, 298, 215-219.
11. Baker, H. M., Day, C. L., Norris, G. E. & Baker, E. N. (1994). Enzymatic deglycosylation as a tool for crystallization of mammalian binding proteins. Acta Crystallog. sect. D, 50, 380-384.
12. Brock, J. H. (1985). Transferrins. In Metalloproteins (Harrison, P., ed.), part 2, pp. 183-262, MacMillan Press, London.
13. Carson, M. & Bugg, C. E. (1986). Algorithm for ribbon models of proteins. J. Mol. Graph. 4, 121-122.
14. Day, C. L., Stowell, K. M., Baker, E. N. & Tweedie, J. W. (1992a). Studies of the N-terminal half of human lactoferrin produced from cloned cDNA demonstrate that interlobe interactions modulate iron release. J. Biol. Chem. 267, 13857-13862.
15. Day, C. L., Norris, G. E., Anderson, B. F., Tweedie, J. W. & Baker, E. N. (1992b). Preliminary crystallographic studies of the amino terminal half of human lactoferrin in its iron-saturated and iron-free forms. J. Mol. Biol. 228, 973-974.
16. Day, C. L., Anderson, B. F., Tweedie, J. W. & Baker, E. N. (1993). Structure of the recombinant N-terminal lobe of human lactoferrin at 2.0 Å resolution. J. Mol. Biol. 232, 1084-1100.
17. Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
18. Evans, R. W., Williams, J. & Moreton, K. (1982). A variant of human transferrin with abnormal properties. Biochem. J. 201, 19-26.
19. Evans, R. W., Meilak, A., Aitken, A., Patel, K. J., Wong, C., Garratt, R. C. & Chitnavis, B. (1988). Characterization of the amino acid change in a transferrin variant. Biochem. Soc. Trans. 16, 834-835.
20. Faber, H. R. & Matthews, B. W. (1990). A mutant T4 lysozyme displays five different crystal conformations. Nature, 348, 263-266.
21. Flocco, M. M. & Mowbray, S. L. (1994). The 1.9 Å X-ray structure of a closed unliganded form of the periplasmic glucose/galactose receptor from Salmonella typhimurium. J. Biol. Chem. 269, 8931-8936.
22. Funk, W. D., MacGillivray, R. T. A., Mason, A. B., Brown, S. A. & Woodworth, R. C. (1990). Expression of the amino-terminal half-molecule of human serum transferrin in cultured cells and characterization of the recombinant protein. Biochemistry, 29, 1654-1660.
23. Gaber, B. P., Miskowski, V. & Spiro, T. G. (1974). Resonance Raman scattering from iron(III) and copper(II)-transferrin and an iron(III) model compound. A spectroscopic interpretation of the transferrin binding site. J. Am. Chem. Soc. 96, 6868-6873.
24. Gerstein, M., Anderson, B. F., Norris, G. E., Baker, E. N., Lesk, A. M. & Chothia, C. (1993). Domain closure in lactoferrin. Two hinges produce a see-saw motion between alternative close-packed interfaces. J. Mol. Biol. 234, 357-372.
25. Gerstein, M., Lesk, A. M. & Chothia, C. (1994). Structural mechanisms for domain movements in proteins. Biochemistry, 33, 6739-6749.
26. Grossmann, J. G., Neu, M., Pantos, E., Schwab, F. J., Evans, R. W., Townes-Andrews, E., Lindley, P. F., Appel, H., Thies W.-G. & Hasnain, S. S. (1992). X-ray solution scattering reveals conformational changes upon iron uptake in lactoferrin, serum and ovotransferrins. J. Mol. Biol. 225, 811-819.
27. Grossmann, J. G., Mason, A. B., Woodworth, R. C., Neu, M., Lindley, P. F. & Hasnain, S. S. (1993). Asp ligand provides the trigger for closure of transferrin molecules. Direct evidence from X-ray scattering studies of site-specific mutants of the N-terminal half-molecule of human transferrin. J. Mol. Biol. 231, 554-558.
28. Haridas, M., Anderson, B. F. & Baker, E. N. (1995). The structure of human diferric lactoferrin, refined at 2.2 Å resolution. Acta Crystallogr. sect. D, 51, 629-646.
29. Harris, D. C. & Aisen, P. (1989). Physical biochemistry of the transferrins. In Iron Carriers and Iron Proteins (Loehr, T. M., ed.), pp. 241-351, U. C. H. Publishers, New York.
30. Hol, W. G. J., van Duijnen, P. T. & Berendsen, H. J. C. (1978). The α-helix dipole and the properties of proteins. Nature, 273, 443-446.
31. r fragment of duck ovotransferrin. J. Mol. Biol. 200, 423-425.
32. Kunkel, T. A., Roberts, J. D. & Zakour, R. A. (1987). Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154, 367-382.
33. Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993). PROCHECK: a program to check stereochemical quality of protein structures. J. Appl. Crystallog. 26, 283-291.
34. Lee, B. & Richards, F. M. (1971). The interpretation of protein structures: estimation of static accessibility J. Mol. Biol. 55, 379-400.
35. Legrand, D., Mazurier, J., Metz-Boutigue, M.-H., Jolles, P., Montreuil, J. & Spik, G. (1984). Characterization and localization of an iron-binding 18 kDa glycopeptide isolated from the N-terminal half of human lactotransferrin. Biochim. Biophys. Acta, 787, 90-96.
36. Lindley, P. F., Bajaj, M., Evans, R. W., Garratt, R. C., Hasnain, S. S., Jhoti, H., Kuser, P., Neu, M., Patel, K., Sarra, R., Strange, R. & Walton, A. (1993). The mechanism of iron uptake by transferrins: the structure of an 18 kDa NII-domain fragment from duck ovotransferrin at 2.3 Å resolution. Acta Crystallog. sect. D, 49, 292-304.
37. Luzzati, V. (1952). Traitements statistiques des erreurs dans la détermination des structures cristallines. Acta Crystallog. 5, 802-810.
38. Matthews, B. W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
39. Matthews, B. W. (1972). The γ-turn. Evidence for a new folded conformation in proteins. Macromolecules, 5, 818-819.
40. Nemethy, G. & Printz, M. P. (1972). The γ-turn, a possible folded conformation of the polypeptide chain. Comparison with the β-turn. Macromolecules, 5, 755-758.
41. Octave, J.-N., Schneider, Y.-J., Trouet, A. & Crichton, R. R. (1983). Iron uptake and utilization by mammalian cells. I: Cellular uptake of transferrin and iron. Trends Biochem. Sci. 8, 217-220.
42. Palmiter, R. D., Behringer, R. R., Quaife, C. J., Maxwell, F., Maxwell, I. H. & Brinster, R. L. (1987). Cell lineage ablation in transgenic mice by cell-specific expression of a toxin gene. Cell, 50, 435-443.
43. Patch, M. G. & Carrano, C. J. (1981). The origin of the visible absorption in metal transferrins. Inorg. Chim. Acta, 56, L71-L73.
44. Presta, L. G. & Rose, G. D. (1988). Helix signals in proteins. Science, 240, 1632-1641.
45. Quiocho, F. A. (1990). Atomic structures of periplasmic binding proteins and the high-affinity active transport systems in bacteria. Phil. Trans. Roy. Soc. ser. B, 326, 341-351.
46. Ramakrishnan, C. & Ramachandran, G. N. (1965). Stereochemical criteria for polypeptide and protein chain conformation. Biophys. J. 5, 909-933.
47. Read, R. J. (1986). Improved Fourier coefficients for maps using phases from partial structures with errors. Acta Crystallog. sect. A, 42, 140-149.
48. Richardson, J. S. & Richardson, D. C. (1988). Amino acid preferences for specific locations at the ends of α helices. Science, 240, 1648-1652.
49. Rose, T. M., Plowman, G. D., Teplow, D. B., Dreyer, W. J., Hellstrōm, K. E. & Brown, J. P. (1986). Primary structure of the human melanoma-associated antigen p97 (melanotransferrin) deduced from the mRNA sequence. Proc. Natl Acad. Sci. USA, 83, 1261-1265.
50. Tronrud, D. E., Ten Eyck, L. F. & Matthews, B. W. (1987). An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A, 43, 489-501.
51. Woodworth, R. C., Mason, A. B., Funk, W. D. & MacGillivray, R. T. A. (1991). Expression and initial characterization of five site-directed mutants of the N-terminal half-molecule of human transferrin. Biochemistry, 30, 10824-10829.
52. Zhang, X.-J. & Matthews, B. W. (1994). Enhancement of the method of molecular replacement by incorporation of known structural information. Acta Crystallog, sect. D, 50, 675-686.