ArticleScientific reports2016
Crystal structure of the vicilin from Solanum melongena reveals existence of different anionic ligands in structurally similar pockets.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Overexpression ofFrontiers in plant science · 2026Article
- Pulse Protein Isolates as Competitive Food Ingredients: Origin, Composition, Functionalities, and the State-of-the-Art Manufacturing.Foods (Basel, Switzerland) · 2023Review
- Asthma-protective agents in dust from traditional farm environments.The Journal of allergy and clinical immunology · 2023Article
- Applications of Enzyme Technology to Enhance Transition to Plant Proteins: A Review.Foods (Basel, Switzerland) · 2023Review
- In Silico Analysis and Functional Characterization of Antimicrobial and Insecticidal Vicilin from Moth Bean (Molecules (Basel, Switzerland) · 2022Article
- Structural characterization and in-silico analysis of Momordica charantia 7S globulin for stability and ACE inhibition.Scientific reports · 2020Article
- Ethnobotany and Antimicrobial Peptides From Plants of the Solanaceae Family: An Update and Future Prospects.Frontiers in pharmacology · 2020Review
- Detect, correct, retract: How to manage incorrect structural models.The FEBS journal · 2018Review
- A novel function for globulin in sequestering plant hormone: Crystal structure of Wrightia tinctoria 11S globulin in complex with auxin.Scientific reports · 2017Article
- Effects of AlProteomes · 2017Article
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3 authors.
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Abstract
Crystal structure of a vicilin, SM80.1, was determined towards exploring its possible physiological functions. The protein was purified from Solanum melongena by combination of ammonium sulphate fractionation and size exclusion chromatography. Structure was determined ab initio at resolution of 1.5 Å by X-ray crystallography showing the three-dimensional topology of the trimeric protein. Each monomer of SM80.1 consists of two similar domains with hydrophobic binding pocket and each accommodating different ligands, i.e. acetate and pyroglutamate. The relatively high stability of these independent anionic ligands in similar pockets indicated a strict requirement of stabilization by hydrogen bonds with the charged residues, suggesting a degree of plasticity within the binding pocket. Comparison of SM80.1 structure with those of other 7S vicilins indicated conservation of putative binding pocket for anionic ligands. Here we propose the possibility of trapping of these ligands in the protein for their requirement in the metabolic processes.
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