1V00

Erythrina cristagalli lectin

Summary for 1V00

• Entry DOI: 10.2210/pdb1v00/pdb
• Related: 1UZY 1UZZ
• Related PRD ID: PRD_900004
• Descriptor: LECTIN (ECL), beta-D-galactopyranose-(1-4)-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: lectin, non-canonical dimer, carbohydrate-binding, sugar binding protein
• Biological source: ERYTHRINA CRISTA-GALLI (COCKSPUR CORAL TREE)
• Total number of polymer chains: 4
• Total formula weight: 108015.36

Authors

Turton, K.,Natesh, R.,Thiyagarajan, N.,Chaddock, J.A.,Acharya, K.R. (deposition date: 2004-03-21, release date: 2004-06-22, Last modification date: 2024-05-08)

Primary citation

Turton, K.,Natesh, R.,Thiyagarajan, N.,Chaddock, J.A.,Acharya, K.R.
Crystal Structures of Erythrina Cristagalli Lectin with Bound N-Linked Oligosaccharide and Lactose
Glycobiology, 14:923-, 2004

PubMed Abstract: Erythrina cristagalli lectin (ECL) is a galactose-specific legume lectin. Although its biological function in the legume is unknown, ECL exhibits hemagglutinating activity in vitro and is mitogenic for T lymphocytes. In addition, it has been recently shown that ECL forms a novel conjugate when coupled to a catalytically active derivative of the type A neurotoxin from Clostridium botulinum, thus providing a therapeutic potential. ECL is biologically active as a dimer in which each protomer contains a functional carbohydrate-combining site. The crystal structure of native ECL was recently reported in complex with lactose and 2'-fucosyllactose. ECL protomers adopt the legume lectin fold but form non-canonical dimers via the handshake motif as was previously observed for Erythrina corallodendron lectin. Here we report the crystal structures of native and recombinant forms of the lectin in three new crystal forms, both unliganded and in complex with lactose. For the first time, the detailed structure of the glycosylated hexasaccharide for native ECL has been elucidated. The structure also shows that in the crystal lattice the glycosylation site and the carbohydrate binding site are involved in intermolecular contacts through water-mediated interactions.

PubMed: 15201215
DOI: 10.1093/GLYCOB/CWH114

Experimental method

X-RAY DIFFRACTION (1.7 Å)