1WUV

Crystal structure of native Canavalia gladiata lectin (CGL): a tetrameric ConA-like lectin

Summary for 1WUV

• Entry DOI: 10.2210/pdb1wuv/pdb
• Descriptor: Concanavalin A, MANGANESE (II) ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: beta sheet structure, native protein, plant protein
• Biological source: Canavalia gladiata (Sword bean); More
• Total number of polymer chains: 4
• Total formula weight: 102633.35

Authors

Freitas, B.T.,Delatorre, P.,Moreno, F.B.M.B.,Rocha, B.A.M.,Souza, E.P.,Canduri, F.,Cardoso, A.L.H.,Sampaio, A.H.,Azevedo Jr., W.F.,Cavada, B.S. (deposition date: 2004-12-09, release date: 2006-04-18, Last modification date: 2023-10-25)

Primary citation

Delatorre, P.,Rocha, B.A.M.,Souza, E.P.,Oliveira, T.M.,Bezerra, G.A.,Moreno, F.B.M.B.,Freitas, B.T.,Santi-Gadelha, T.,Sampaio, A.H.,Azevedo Jr., W.F.,Cavada, B.S.
Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
Bmc Struct.Biol., 7:52-52, 2007

PubMed Abstract: 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.

PubMed: 17683532
DOI: 10.1186/1472-6807-7-52

Experimental method

X-RAY DIFFRACTION (2.3 Å)