Crystal structures and structural stabilities of the disulfide bond-deficient soybean proglycinin mutants C12G and C88S

Journal of Agricultural and Food Chemistry

Volumn 51, Issue 16, 2003, Pages 4633-4639

  Adachi, Motoyasu ^a   Okuda, Eiko ^a   Kaneda, Yumiko ^a   Hashimoto, Asako ^a   Shutov, Andrei D ^b   Becker, Claudia ^c   Müntz, Klaus ^c   Utsumi, Shigeru ^a  

^a KYOTO UNIVERSITY   (Japan)

^b MOLDOVA STATE UNIVERSITY   (Moldova)

^c LEIBNIZ INSTITUTE OF PLANT GENETICS AND CROP PLANT RESEARCH IPK   (Germany)

Author keywords

Crystal structure; Disulfide bond deficient; Proglycinin; Soybean; Structural stability

Indexed keywords

GLOBULIN; GLYCININ; PROGLYCININ; SOYBEAN PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CRYSTAL STRUCTURE; DIFFERENTIAL SCANNING CALORIMETRY; DISULFIDE BOND; LEGUME; MUTAGENESIS; NONHUMAN; PROTEIN CONFORMATION; PROTEIN STABILITY; SEED STORAGE; SOYBEAN; STRUCTURE ANALYSIS; THERMOSTABILITY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CALORIMETRY, DIFFERENTIAL SCANNING; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; DISULFIDES; DRUG STABILITY; GLOBULINS; HEAT; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS; PROTEIN CONFORMATION; PROTEIN PRECURSORS; SERINE ENDOPEPTIDASES; SOYBEAN PROTEINS; SOYBEANS;

GLYCINE MAX;

EID: 0042303912     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf026065y     Document Type: Article

References (35)

1. Utsumi, S.; Matsumura, Y.; Mori, T. Structure-function relationships of soy proteins. In Food Proteins and Their Applications; Damodaran, S., Paraf, A., Eds.; Dekker: New York, 1997; pp 257-291.
2. Shewry, P. R.; Napier, J. A.; Tatham, A. S. Seed storage proteins: structure and biosynthesis. Plant Cell 1995, 7, 945-956.
3. Lawrence, M. C.; Suzuki, E.; Varghese, J. N.; Davis, P. C.; Van Donkelaar, A.; Tulloch, P. A.; Colman, P. M. The three-dimensional structure of the seed storage protein phaseolin at 3 Å resolution. EMBO J. 1990, 9, 9-15.
4. Lawrence, M. C.; Izard, T.; Beuchat, M.; Blagrobe, R. J.; Colman, P. M. Structure of phaseolin at 2.2 Å resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J. Mol. Biol. 1994, 238, 748-776.
5. Ko, T.-P.; Ng, J. D.; McPherson, A. The three-dimensional structure of canavalin from jack bean (Canavalia ensiformis). Plant Physiol. 1993, 101, 729-744.
6. Ko, T.-P.; Day, J.; McPherson, A. The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 Å resolution. Acta Crystallogr. D 2000, 56, 411-420.
7. Adachi, M.; Takenaka, Y.; Gidamis, A. B.; Mikami, B.; Utsumi, S. Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 2001, 305, 291-305.
8. Maruyama, N.; Adachi, M.; Takahashi, K.; Yagasaki, K.; Kohno, M.; Takenaka, Y.; Okuda, E.; Nakagawa, S.; Mikami, B.; Utsumi, S. Crystal structures of recombinant and native soybean β-conglycinin β homotrimers. Eur. J. Biochem. 2001, 268, 3595-3604.
9. Utsumi, S.; Gidamis, A. B.; Kanamori, J.; Kang, I. J.; Kito, M. Effects of deletion of disulfide bonds by protein engineering on the conformation and functional properties of soybean proglycinin. J. Agric. Food Chem. 1993, 41, 687-691.
10. Fersht, A. R.; Serrano, L. Principles of protein stability derived from protein engineering experiments. Curr. Opin. Struct. Biol. 1993, 3, 75-83.
11. Bonander, N.; Leckner, J.; Guo, H.; Karlsson, B. G.; Sjölin, L. Crystal structure of the disulfide bond-deficient azurin mutant C3A/C26A. Eur. J. Biochem. 2000, 267, 4511-4519.
12. Scott, M. P.; Jung, R.; Müntz, K.; Nielsen, N. C. A protease responsible for post-translational cleavage of a conserved Asn-Gly linkage in glycinin, the major seed storage protein of soybean. Proc. Natl. Acad. Sci. U.S.A. 1992, 89, 658-662.
13. Shimada, T.; Hiraiwa, N.; Nishimura, M.; Hara-Nishimura, I. Vacuolar processin enzyme of soybean that converts proproteins to the corresponding mature forms. Plant Cell Physiol. 1994, 35, 713-718.
14. Momma, T.; Negoro, T.; Hirano, H.; Matsumoto, A.; Udaka, K.; Fukazawa, C. Glycinin A5A4B3 mRNA: cDNA cloning and nucleotide sequencing of a splitting storage protein subunit of soybean. Eur. J. Biochem. 1985, 149, 491-496.
15. Yanish-Perron, C.; Vieira, J.; Messing, J. Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13mp18 and pUC19 vectors. Gene 1985, 33, 103-119.
16. Utsumi, S.; Kim, C.-S.; Sato, T.; Kito, M. Signal sequence of preproglycinin affects production of the expressed protein in Escherichia coli. Gene 1988, 71, 349-358.
17. Kim, C.-S.; Kamiya, S.; Kanamori, J.; Utsumi, S.; Kito, M. High-level expression, purification and functional properties of soybean proglycinin from Escherichia coli. Agric. Biol. Chem. 1990, 54, 1546-1550.
18. Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
19. Gidamis, A. B.; Mikami, B.; Katsube, T.; Utsumi, S.; Kito, M. Crystallization and preliminary X-ray analysis of soybean proglycinins modified by protein engineering. Biosci., Biotechnol., Biochem. 1994, 58, 703-706.
20. Maruyama, N.; Katsube, T.; Wada, Y.; Oh, M. H.; Barba dela Rosa, A. P.; Okuda, E.; Nakagawa, S.; Utsumi, S. The roles of the N-linked glycans and extension regions of soybean β-conglycinin in folding, assembly and structural features. Eur. J. Biochem. 1998, 258, 854-862.
21. Becker, C.; Shutov, A. D.; Nong, V. H.; Senyuk, V. I.; Jung, R.; Horstmann, C.; Fischer, J.; Nielsen, N. C.; Müntz, K. Purification, cDNA cloning and characterization of proteinase B, an asparagine-specific endopeptidase from germinating vetch (Vicia sativa L.) seeds. Eur. J. Biochem. 1995, 228, 456-462.
22. Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227, 680-685.
23. Matsudaira, P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 1987, 262, 10035-10038.
24. Freire, E.; van Osdol, W. W.; Mayorga, O. L.; Sánchez-Ruíz, J. M. Annu. Rev. Biophys. Chem. 1990, 19, 159-188.
25. Jung, R.; Nam, Y.-W.; Saalbach, I.; Müntz, K.; Nielsen, N. C. Role of the sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins. Plant Cell 1997, 9, 2037-2050.
26. Branden, C.; Tooze, J. Introduction to Protein Structure; Garland Publishing: New York, 1991.
27. Klink, T. A.; Woycechowsky, K. J.; Yaylor, K. M.; Raines, R. T. Contribution of disulfide bonds to the conformational stability and catalytic activity of ribonuclease A. Eur. J. Biochem. 2000, 267, 566-572.
28. Kanaya, S.; Katsuda, C.; Kimura, S.; Nakai, T.; Kitakuni, E.; Nakamura, H.; Katayanagi, K.; Morikawa, K.; Ikehara, M. Stabilization of Escherichia coli ribonuclease H by introduction of an artificial disulfide bond. J. Biol. Chem. 1991, 266, 6038-6044.
29. Mansfeld, J.; Vriend, G.; Dijkstra, B. W.; Veltman, O. R.; Van den Burg, B.; Venema, G.; Ulbrich-Hofmann, R.; Eijsink, V. G. H. Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond. J. Biol. Chem. 1997, 272, 11152-11156.
30. Kabashima, T.; Li, Y.; Kanada, N.; Ito, K.; Yoshimoto, T. Enhancement of the thermal stability of pyroglutamyl peptidase I by introduction of an intersubunit disulfide bond. Biochim. Biophys. Acta 2001, 1547, 214-220.
31. Halfon, S.; Patel, S.; Vega, F.; Zurawski, S.; Zurawski, G. Autocatalytic activation of fuman legumain at aspartic acid residues. FEBS Lett. 1998, 438, 114-118.
32. Hiraiwa, N.; Nishimura, M.; Hara-Nishimura, I. Vacuolar processing enzyme is self-catalytically acitivated by sequential removal of the C-terminal and N-terminal propeptides. FEBS Lett. 1999, 447, 213-216.
33. Rotari, V. I.; Dando, P. M.; Barrett, A. J. Legumain forms from plants and animals differ in their specificity. J. Biol. Chem. 2001, 382, 953-959.
34. Matsumura, M.; Signor, G.; Matthews, B. W. Substantial increase of protein stability by multiple disulfide bonds. Nature 1989, 342, 291-293.
35. Kraulis, P. MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 1991, 24, 946-950.