2EIG

Lotus tetragonolobus seed lectin (Isoform)

Summary for 2EIG

• Entry DOI: 10.2210/pdb2eig/pdb
• Descriptor: lectin, 2-acetamido-2-deoxy-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: lotus tetragonolobus, l-fucosyl, n-acetyl-d-glucosamine, sugar binding protein
• Biological source: Lotus tetragonolobus (winged pea)
• Total number of polymer chains: 4
• Total formula weight: 105175.32

Authors

Moreno, F.B.M.B.,Vicoti, M.M.,Abrego, J.R.B.,de Oliveira, T.M.,Bezerra, G.A.,Cavada, B.S.,Filgueira de Azevedo Jr., W. (deposition date: 2007-03-13, release date: 2008-03-04, Last modification date: 2024-10-23)

Primary citation

Moreno, F.B.M.B.,de Oliveira, T.M.,Martil, D.E.,Vicoti, M.M.,Bezerra, G.A.,Abrego, J.R.B.,Cavada, B.S.,Filgueira de Azevedo Jr., W.
Identification of a new quaternary association for legume lectins
J.Struct.Biol., 161:133-143, 2008

PubMed Abstract: Lotus tetragonolobus lectin (LTA) is a fucose-specific legume lectin. Although several studies report a diverse combination of biological activities for LTA, little is known about the mechanisms involved in l-fucosyl oligosaccharide recognition. The crystal structure of LTA at 2.0A resolution reveals a different legume lectin tetramer. Its structure consists of a homotetramer composed of two back-to-back GS4-like dimers arranged in a new mode, resulting in a novel tetramer. The LTA N-linked carbohydrate at Asn4 and the unusual LTA dimer-dimer interaction are related to its particular mode of tetramerization. In addition, we used small angle X-ray scattering to investigate the quaternary structure of LTA in solution and to compare it to the crystalline structure. Although the crystal structure of LTA has revealed a conserved metal-binding site, its l-fucose-binding site presents some punctual differences. Our investigation of the new tetramer of LTA and its fucose-binding site is essential for further studies related to cross-linking between LTA and complex divalent l-fucosyl carbohydrates.

PubMed: 18068379
DOI: 10.1016/j.jsb.2007.10.002

Experimental method

X-RAY DIFFRACTION (2 Å)