2ZBJ

Crystal structure of Dioclea rostrata lectin

Summary for 2ZBJ

• Entry DOI: 10.2210/pdb2zbj/pdb
• Descriptor: Lectin alpha chain, PHOSPHATE ION, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: leguminosae, lectin, diocleinae, dioclea rostrata, calcium, manganese, metal-binding, vacuole, sugar binding protein
• Biological source: Dioclea rostrata
• Cellular location: Vacuole, aleurone grain: P58908
• Total number of polymer chains: 1
• Total formula weight: 25703.18

Authors

de Oliveira, T.M.,Delatorre, P.,da Rocha, B.A.M.,de Sousa, E.P.,Nascimento, K.S.,Bezerra, G.A.,Moura, T.R.,Benevides, R.G.,Bezerra, E.H.S.,Moreno, F.B.M.B.,Freire, V.N.,de Azevedo Jr., W.F.,Cavada, B.S. (deposition date: 2007-10-22, release date: 2008-08-19, Last modification date: 2023-11-01)

Primary citation

de Oliveira, T.M.,Delatorre, P.,da Rocha, B.A.M.,de Souza, E.P.,Nascimento, K.S.,Bezerra, G.A.,Moura, T.R.,Benevides, R.G.,Bezerra, E.H.S.,Moreno, F.B.M.B.,Freire, V.N.,de Azevedo Jr., W.F.,Cavada, B.S.
Crystal structure of Dioclea rostrata lectin: Insights into understanding the pH-dependent dimer-tetramer equilibrium and the structural basis for carbohydrate recognition in Diocleinae lectins
J.Struct.Biol., 164:177-182, 2008

PubMed Abstract: The legume lectins from the subtribe Diocleinae, often referred to as concanavalin A-like lectins, are a typical example of highly similar proteins that show distinct biological activities. The pH-dependent oligomerization that some of these lectins undergo and the relative position of amino acids within the carbohydrate-binding site are factors that have been reported to contribute to these differences in the activities of Diocleinae lectins. In the present work, we determined the amino acid sequence and the crystal structure of the lectin of Dioclea rostrata seeds (DRL), with the aim of investigating the structural bases of the different behavior displayed by this lectin in comparison to other Diocleinae lectins and determining the reason for the distinct pH-dependent dimer-tetramer equilibrium. In addition, we discovered a novel multimeric arrangement for this lectin.

PubMed: 18682294
DOI: 10.1016/j.jsb.2008.05.012

Experimental method

X-RAY DIFFRACTION (2.05 Å)