Structure of a Lectin from Canavalia Gladiata Seeds: New Structural Insights for Old Molecules.
From: Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Ceará, Brazil. plinio@urca.br
BMC structural biology
- Publish Date: 2007
- ISSN: 1472-6807
- Volume: 7
- Issue:
- Pages: 52
- Medium: Internet
- Language: English
- Citation (JAMA): Delatorre Plínio, Rocha Bruno A M, Souza Emmanuel P, et al. Structure of a Lectin from Canavalia Gladiata Seeds: New Structural Insights for Old Molecules.. BMC Struct. Biol. 2007;7:52
Abstract
BACKGROUND: Lectins are mainly described as simple carbohydrate-binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds (CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA-like lectins; a site where a non-protein amino-acid, alpha-aminobutyric acid (Abu), is bound. RESULTS: The overall structure of native CGL and complexed with alpha-methyl-mannoside and Abu have been refined at 2.3 A and 2.31 A resolution, respectively. Analysis of the electron density maps of the CGL structure shows clearly the presence of Abu, which was confirmed by mass spectrometry. CONCLUSION: The presence of Abu in a plant lectin structure strongly indicates the ability of lectins on carrying secondary metabolites. Comparison of the amino acids composing the site with other legume lectins revealed that this site is conserved, providing an evidence of the biological relevance of this site. This new action of lectins strengthens their role in defense mechanisms in plants.
Mesh Headings (Keywords): Aminobutyric Acids, Binding Sites, Canavalia, Crystallography, X-Ray, Hydrophobicity, Models, Molecular, Plant Lectins, Protein Binding, Protein Conformation, Protein Structure, Tertiary, Seeds, Spectrometry, Mass, Electrospray Ionization
Check for Full Text / PubMed Unique Identifier (PMID): 17683532
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