Structure of a putative ancestral protein encoded by a single sequence repeat from a multidomain proteinase inhibitor gene from Nicotiana alata

Structure

Volumn 7, Issue 7, 1999, Pages 793-802

  Scanlon, Martin J ^a   Lee, Marcus CS ^b,c   Anderson, Marilyn A ^b   Craik, David J ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b LA TROBE UNIVERSITY   (Australia)

^c UNIVERSITY OF MELBOURNE   (Australia)

Author keywords

Nicotiana alata; NMR spectroscopy; Proteinase inhibitor

Indexed keywords

VEGETABLE PROTEIN;

ARTICLE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PHYTOCHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

NICOTIANA ALATA;

EID: 0033565476     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(99)80103-8     Document Type: Article

References (40)

1. Atkinson, A.H., Heath, R.L., Simpson, R.J., Clarke, A.E. & Anderson, M.A. (1993). Proteinase inhibitors in Nicotiana alata stigmas are derived from a precursor protein which is processed into five homologous inhibitors. Plant Cell 5, 203-213.
2. Nielsen, K.J., Hill, J.M., Anderson, M.A. & Craik, D.J. (1996). Synthesis and structure determination by NMR of a putative vacuolar targeting peptide and model of a proteinase inhibitor from Nicotiana alata. Biochemistry 35, 369-378.
3. Heath, R.L., Barton, P.A., Simpson, R.J., Reid, G.E., Lim, G. & Anderson, M.A. (1995). Characterization of the protease processing sites in a multidomain proteinase inhibitor precursor from Nicotiana alata. Eur. J. Biochem. 230, 250-257.
4. Lee, M.C.S., Scanlon, M.J., Craik, D.J. & Anderson, M.A. (1999). A novel two-chain proteinase inhibitor generated by circularization of a multidomain precursor protein. Nat. Struct. Biol., in press.
5. Bryant, J., Green, T.R., Gurusaddaiah, T. & Ryan, C.A. (1976). Proteinase inhibitor II from potatoes: Isolation and characterization of its protomer components. Biochemistry 15, 3418-3424.
6. Plunkett, G., Senear, D.F., Zuroske, G. & Ryan, C.A. (1982). Proteinase inhibitors I and II from leaves of wounded tomato plants: Purification and properties. Arch. Biochem. Biophys. 213, 463-472.
7. Balandin, T., van der Does, C., Albert, J.M., Bol, J.F. & Linthorst, H.J. (1995). Structure and induction pattern of a novel proteinase inhibitor class II gene of tobacco. Plant Mol. Biol. 27, 1197-1204.
8. Graham, J.S., Pearce, G., Merryweather, J., Titani, K., Ericsson, L.H. & Ryan, C.A. (1985). Wound-induced proteinase inhibitors from tomato leaves. II. The cDNA-deduced primary structure of pre-inhibitor II. J. Biol. Chem. 260, 6561-6564.
9. Greenblatt, H.M., Ryan, C.A. & James, M.N. (1989). Structure of the complex of Streptomyces griseus proteinase B and polypeptide chymotrypsin inhibitor-1 from Russet Burbank potato tubers at 2.1 Å resolution. J. Mol. Biol. 205, 201-228.
10. Wüthrich, K. (1986). NMR of Proteins and Nucleic Acids. John Wiley & Sons Inc., New York.
11. Guntert, P., Mumenthaler, C. & Wüthrich, K. (1997). Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298.
12. Pallaghy, P.K., Duggan, B.M., Pennington, M.W. & Norton, R.S. (1993). Three-dimensional structure in solution of the calcium channel blocker w-conotoxin. J. Mol. Biol. 234, 405-420.
13. Laskowski, R.A., Rullmannn, J.A., MacArthur, M.W., Kaptein, R. & Thornton, J.M. (1996). AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8, 477-486.
14. Hutchinson, E.G. & Thornton, J.M. (1996). PROMOTIF - A program to identify and analyse structural motifs in proteins. Protein Sci. 5, 212-220.
15. 1H NMR of a 6-kDa proteinase inhibitor isolated from the stigma of Nicotiana alata. J. Mol. Biol. 242, 231-243.
16. Nielsen, K.J., Heath, R.L., Anderson, M.A. & Craik, D.J. (1995). Structures of a series of 6-kDa trypsin inhibitors isolated from the stigma of Nicotiana alata. Biochem. 34, 14304-14311.
17. Lindqvist, Y. & Schneider, G. (1997). Circular permutations of natural protein sequences: Structural evidence. Curr. Opin. Struct. Biol. 7, 422-427.
18. Heinemann, U. & Hahn, M. (1995). Circular permutation of polypeptide chains: Implications for protein folding and stability. Prog. Biophys. Mol. Biol. 64, 121-143.
19. Horlick, R.A., et al., & Horuk, R. (1992). Permuteins of interleukin 1 β - A simplified approach for the construction of permutated proteins having new termini. Protein Eng. 5, 427-431.
20. Buchwalder, A., Szadkowski, H. & Kirschner, K. (1992). A fully active variant of dihydrofolate reductase with a circularly permuted sequence. Biochemistry 31, 1621-1630.
21. Protasova, N., et al., & Gudkov, AT. (1994). Circularly permuted dihydrofolate reductase of E. coli has functional activity and a destabilized tertiary structure. Protein Eng. 7, 1373-1377.
22. Viguera, A.R., Blanco, F.J. & Serrano, L. (1995). The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics. J. Mol. Biol. 247, 670-681.
23. Guruprasad, K., Tormakangas, K., Kervinen, J. & Blundell, T.L. (1994). Comparative modelling of barley-grain aspartic proteinase: A structural rationale for observed hydrolytic specificity. FEBS Lett. 352, 131-136.
24. Ponting, C.P. & Russell, R.B. (1995). Swaposins: Circular permutations within genes encoding saposin homologues. Trends Biochem. Sci. 20, 179-180.
25. Sambrook, J., Fritsch, E.F. & Maniatis, T. (1989). Molecular Cloning, a Laboratory Manual. Cold Spring Harbour Laboratory Press, New York.
26. 1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113, 967-974.
27. 1H NMR spectra of proteins via double quantum filtering. Biochem. Biophys. Res. Comm. 117, 479-485.
28. Braunschweiler, L. & Ernst, R.R. (1983). Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy. J. Magn. Reson. 53, 521-528.
29. Bax, A. & Davis, D.G. (1985). MLEV-17 based two dimensional homonuclear magnetisation transfer spectroscopy. J. Magn. Reson. 65, 355-360.
30. Greisinger, C., Sarenson, O.W. & Ernst, R.R. (1987). Practical aspects of the E.COSY technique: Measurement of scalar spin-spin coupling constants in peptides. J. Magn. Reson. 88, 177-185.
31. Kumar, A., Ernst, R.R. & Wüthrich, K. (1980). A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95, 1-6.
32. Piotto, M., Saudek, V. & Sklenar, V. (1992). Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2, 661-665.
33. Bartels, C.H., Xia, T.-H., Billeter, M., Güntert, P. & Wüthrich, K. (1995). The program XEASY for computer supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 5, 1-10.
34. Stein, E.G., Rice, L.M. & Brünger, A.T. (1997). Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation. J. Magn. Reson. 124, 154-164.
35. Brünger, A.T. (1992). X-PLOR Version 3.1. A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
36. Nilges, M., Gronenborn, A.M., Brünger, A.T. & Clore, G.M. (1988). Determination of three-dimensional structures of proteins by simulated annealing with interproton distance constraints. Application to crambin, potato carboxypeptidase inhibitor and barley serine proteinase inhibitor 2. Protein Eng. 2, 27-38.
37. Garrett, D.S., et al., & Clore, G.M. (1994). The impact of direct refinement against three-bond HN-CαH coupling constants on protein structure determination by NMR. J. Magn. Reson. B 104, 99-103.
38. Kuszewski, J., Gronenborn, A.M. & Clore, G.M. (1995). The impact of direct refinement against proton chemical shifts on protein structure determination by NMR. J. Magn. Reson. B 107, 293-297.
39. Brooks, B.R., Bruccoleri, R.E., Olafson, B.D., States, D.J., Swaminathan, S. & Karplus, M. (1983). CHARMm: A program for macromolecular energy minimisation and dynamics calculations. J. Comput. Chem. 4, 187-217.
40. Koradi, R., Billeter, M. & Wüthrich, K. (1996). MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55.