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Solution structure of .gamma.1-H and .gamma.1-P thionins from barley and wheat endosperm determined by proton NMR: a structural motif common to toxic arthropod proteins
Abstract
The complete assignment of the proton NMR spectra of the homologous gamma 1-hordothionin and gamma 1-purothionin (47 amino acids, 4 disulfide bridges) from barley and wheat, respectively, has been performed by two-dimensional sequence-specific methods. A total of 299 proton-proton distance constraints for gamma 1-H and 285 for gamma 1-P derived from NOESY spectra have been used to calculate the three-dimensional solution structures. Initial structures have been generated by distance geometry methods and further refined by dynamical simulated annealing calculations. Both proteins show identical secondary and tertiary structure with a well-defined triple-stranded antiparallel beta-sheet (residues 1-6, 31-34, and 39-47), an alpha-helix (residues 16-28), and the corresponding connecting loops. Three disulfide bridges are located in the hydrophobic core holding together the alpha-helix and the beta-sheet and forming a cysteine-stabilized alpha-helical (CSH) motif. Moreover, a clustering of positive charges is observed on the face of the beta-sheet opposite to the helix. The three-dimensional structures of the gamma-thionins differ remarkably from plant alpha- and beta-thionins and crambin. However, they show a higher structural analogy with scorpion toxins and insect defensins which also present the CSH motif.
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Cited by
Plant pathogenesis-related (PR) proteins: A focus on PR peptides
Sels, J., Mathys, J., De Coninck, B. M. A., Cammue, B. P. A., & De Bolle, M. F. C. (2008) · Plant Physiology and Biochemistry · doi:10.1016/j.plaphy.2008.06.011 · Cited by 836
Antimicrobial Peptides from Plants
Broekaert, W. F., Cammue, B. P. A., De Bolle, M. F. C., Thevissen, K., De Samblanx, G. W., Osborn, R. W., & Nielson, K. (1997) · Critical Reviews in Plant Sciences · doi:10.1080/07352689709701952 · Cited by 678
Small cysteine-rich antifungal proteins from radish: their role in host defense.
Terras, F. R., Eggermont, K., Kovaleva, V, Raikhel, N. V., Osborn, R. W., Kester, A., Rees, S. B., Torrekens, S., Van Leuven, F., & Vanderleyden, J. (1995) · The Plant Cell · doi:10.1105/tpc.7.5.573 · Cited by 665
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Disease Resistance Mechanisms in Plants
Andersen, E. J., Ali, S., Byamukama, E., Yen, Y., & Nepal, M. P. (2018) · Genes · doi:10.3390/genes9070339 · Cited by 434
Metadata
- Authors
- Bruix, M., Jimenez, M. A., Santoro, J., Gonzalez, C., Colilla, F. J., Mendez, E., & Rico, M.
- Venue
- Biochemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 1993-01-19
- Volume
- 32
- Issue
- 2
- Pages
- 715-724
- ISSN
- 0006-2960 (ISSN-L)
- 1520-4995
- OpenAlex
- W2053265129
- Cited by
- 207
- References
- 0
- FWCI
- 4.00
- Type
- journal article
- Language
- en
- Open access
- closed
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- CoChat. (2026). Citation check: Solution structure of .gamma.1-H and .gamma.1-P thionins from barley and wheat endosperm determined by proton NMR: a structural motif common to toxic arthropod proteins. https://app.cochat.ai/papers/10.1021/bi00053a041
- The paper
- Bruix, M., Jimenez, M. A., Santoro, J., Gonzalez, C., Colilla, F. J., Mendez, E., & Rico, M. (1993). Solution structure of .gamma.1-H and .gamma.1-P thionins from barley and wheat endosperm determined by proton NMR: a structural motif common to toxic arthropod proteins. Biochemistry. https://doi.org/10.1021/bi00053a041
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