PDBsum entry 1v00

Sugar binding protein

PDB id: 1v00

Contents

Protein chains

240 a.a. *

Ligands

BGC-GAL ×4

Metals

_CA ×4

_MN ×4

Waters ×1119

* Residue conservation analysis

PDB id:

1v00

Name:

Sugar binding protein

Title:

Erythrina cristagalli lectin

Structure:

Lectin (ecl). Chain: a, b, c, d. Engineered: yes

Source:

Erythrina crista-galli. Cockspur coral tree. Organism_taxid: 49817. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: legume seeds

Biol. unit:

Dimer (from PDB file)

Resolution:

1.70Å R-factor: 0.172 R-free: 0.195

Authors:

K.Turton,R.Natesh,N.Thiyagarajan,J.A.Chaddock,K.R.Acharya

Key ref:

K.Turton et al. (2004). Crystal structures of Erythrina cristagalli lectin with bound N-linked oligosaccharide and lactose. Glycobiology, 14, 923-929. PubMed id: 15201215

Date:

21-Mar-04 Release date: 22-Jun-04

Protein chains

Q6YD91  (Q6YD91_ERYCG) -  Lectin (Fragment) from Erythrina crista-galli

Seq: 242 a.a.

Struc: 240 a.a.

Enzyme reactions

• Enzyme class: E.C.?

Glycobiology 14:923-929 (2004)

PubMed id: 15201215

Crystal structures of Erythrina cristagalli lectin with bound N-linked oligosaccharide and lactose.

K.Turton, R.Natesh, N.Thiyagarajan, J.A.Chaddock, K.R.Acharya.

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.