The Kunitz-type trypsin inhibitor from seeds of Flamboyant (Delonix regia) has been purified to homogeneity and plate-like crystals suitable for X-ray analysis have been grown by the hanging-drop method using PEG 6000 as a precipitant. The crystals belong to space group P2(1)2(1)2(1) with unit-cell parameters a = 32.15, b = 69.39, c = 72.54 A. X-ray diffraction data have been collected to 2.95 A resolution. The structure has been solved by molecular replacement using the known structures of trypsin inhibitors from Erythrina caffra seeds (PDB code 1tie) and from soya beans (Glycine max; PDB code 1ba7) as search models.
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http://dx.doi.org/10.1107/s0907444999009361 | DOI Listing |
Int J Mol Sci
December 2024
Key Laboratory for Forest Genetics and Tree Improvement and Propagation in University of Yunnan Province, Southwest Forestry University, Kunming 650224, China.
Plant protease inhibitors are a ubiquitous feature of plant species and exert a substantial influence on plant stress responses. However, the (Kunitz trypsin inhibitor) family responding to abiotic stress has not been fully characterized in . In this study, we conducted a genome-wide study of the family and analyzed their gene structure, gene duplication, conserved motifs, cis-acting elements, and response to stress treatment.
View Article and Find Full Text PDFProtein J
December 2024
Plant Genetic Resources and Improvement Division, CSIR-National Botanical Research Institute, Lucknow, Uttar Pradesh, India.
Trypsin inhibitor from the root-tuber of underutilized legume Winged bean (Psophocarpus tetragonolobus (L.) DC.) (WbT-TI) was purified using ion exchange chromatography followed by size-exclusion chromatography.
View Article and Find Full Text PDFToxins (Basel)
November 2024
Animal Toxin Group, Engineering Research Center of Active Substance and Biotechnology, Ministry of Education, College of Life Science, Chongqing Normal University, Chongqing 401331, China.
Kraits are venomous snakes of the genus from the family . Their venom typically demonstrates neurotoxicity; however, the toxicity is significantly influenced by the snake's species and geographical origin. Among the species, and have been poorly studied, with little to no information available regarding their venom composition.
View Article and Find Full Text PDFProtein Sci
December 2024
Center of Excellence for Molecular Biology and Genomics of Shrimp, Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok, Thailand.
Kunitz-type trypsin inhibitors are ubiquitous in plants. They have been proposed to be a part of a defense mechanism against herbivores. Trypsin inhibitors also have potential applications in the biotechnology industry, such as in mammalian cell culture.
View Article and Find Full Text PDFComput Struct Biotechnol J
December 2024
Institute of Botany, Bahauddin Zakariya University, Multan 60800, Pakistan.
Trypsin inhibitors are known to act against insect pests by inhibiting proteases of the digestive tract. In this study, we report structural and functional characterization of ∼ 19 kDa Kunitz-type trypsin inhibitor (ApKTI) protein with potential bio-insecticidal applications. Crystal structure of ApKTI protein has been refined to 1.
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