Glycobiology Advance Access originally published online on June 16, 2004
Glycobiology 2004 14(10):923-929; doi:10.1093/glycob/cwh114
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Glycobiology vol. 14 no. 10 © Oxford University Press 2004; all rights reserved.
Crystal structures of Erythrina cristagalli lectin with bound N-linked oligosaccharide and lactose
3 Department of Biology and Biochemistry, University of Bath, Claverton Down, Bath BA2 7AY, United Kingdom, and 4 The Health Protection Agency, Porton Down, Salisbury SP4 0JG, United Kingdom
Received on April 19, 2004; revised on June 1, 2004; accepted on June 11, 2004
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.
1 Present address: ICGEB, Aruna Asaf Ali Marg, New Delhi 110 067, India
2 To whom correspondence should be addressed; e-mail: k.r.acharya{at}bath.ac.uk
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