4K20

Crystal structure of Canavalia boliviana lectin

Summary for 4K20

• Entry DOI: 10.2210/pdb4k20/pdb
• Related: 4K1Y 4K1Z 4K21
• Descriptor: Canavalia boliviana lectin, MANGANESE (II) ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: diocleinae lectins, dimannosides, oligomerization, binding sites, jelly roll, carbohydrate binding, mannose binding protein
• Biological source: Canavalia boliviana
• Total number of polymer chains: 2
• Total formula weight: 51382.79

Authors

Viertlmayr, R.,Bezerra, G.A.,Moura, T.R.,Delatorre, P.,Rocha, B.A.M.,Cavada, B.S.,Gruber, K. (deposition date: 2013-04-07, release date: 2014-04-09, Last modification date: 2024-02-28)

Primary citation

Bezerra, G.A.,Viertlmayr, R.,Moura, T.R.,Delatorre, P.,Rocha, B.A.,do Nascimento, K.S.,Figueiredo, J.G.,Bezerra, I.G.,Teixeira, C.S.,Simoes, R.C.,Nagano, C.S.,de Alencar, N.M.,Gruber, K.,Cavada, B.S.
Structural Studies of an Anti-Inflammatory Lectin from Canavalia boliviana Seeds in Complex with Dimannosides.
Plos One, 9:e97015-e97015, 2014

PubMed Abstract: Plant lectins, especially those purified from species of the Leguminosae family, represent the best-studied group of carbohydrate-binding proteins. Lectins purified from seeds of the Diocleinae subtribe exhibit a high degree of sequence identity notwithstanding that they show very distinct biological activities. Two main factors have been related to this feature: variance in key residues influencing the carbohydrate-binding site geometry and differences in the pH-dependent oligomeric state profile. In this work, we have isolated a lectin from Canavalia boliviana (Cbol) and solved its x-ray crystal structure in the unbound form and in complex with the carbohydrates Man(α1-3)Man(α1-O)Me, Man(α1-4)Man(α1-O)Me and 5-bromo-4-chloro-3-indolyl-α-D-mannose. We evaluated its oligomerization profile at different pH values using Small Angle X-ray Scattering and compared it to that of Concanavalin A. Based on predicted pKa-shifts of amino acids in the subunit interfaces we devised a model for the dimer-tetramer equilibrium phenomena of these proteins. Additionally, we demonstrated Cbol anti-inflammatory properties and further characterized them using in vivo and in vitro models.

PubMed: 24865454
DOI: 10.1371/journal.pone.0097015

Experimental method

X-RAY DIFFRACTION (3.4 Å)