PDBsum entry 3wmv

Sugar binding protein

PDB id: 3wmv

Contents

Protein chains

150 a.a.

Ligands

A2G ×6

Waters ×299

PDB id:

3wmv

Name:

Sugar binding protein

Title:

The structure of an anti-cancer lectin mytilec with ligand from the mussel mytilus galloprovincialis

Structure:

Lectin. Chain: a, b. Synonym: mytilec. Engineered: yes. Mutation: yes

Source:

Mytilus galloprovincialis. Mediterranean mussel. Organism_taxid: 29158. Expressed in: escherichia coli. Expression_system_taxid: 562

Resolution:

1.05Å R-factor: 0.137 R-free: 0.155

Authors:

D.Terada,F.Kawai,H.Noguchi,S.Unzai,S.-Y.Park,Y.Ozeki,J.R.H.Tame

Key ref:

D.Terada et al. (2016). Crystal structure of MytiLec, a galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types. Sci Rep, 6, 28344. PubMed id: 27321048

Date:

27-Nov-13 Release date: 03-Dec-14

Protein chains

B3EWR1  (LEC1_MYTGA) -  Alpha-D-galactose-binding lectin from Mytilus galloprovincialis

Seq: 187 a.a.

Struc: 150 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

Sci Rep 6:28344 (2016)

PubMed id: 27321048

Crystal structure of MytiLec, a galactose-binding lectin from the mussel Mytilus galloprovincialis with cytotoxicity against certain cancer cell types.

D.Terada, F.Kawai, H.Noguchi, S.Unzai, I.Hasan, Y.Fujii, S.Y.Park, Y.Ozeki, J.R.Tame.

ABSTRACT

MytiLec is a lectin, isolated from bivalves, with cytotoxic activity against cancer cell lines that express globotriaosyl ceramide, Galα(1,4)Galβ(1,4)Glcα1-Cer, on the cell surface. Functional analysis shows that the protein binds to the disaccharide melibiose, Galα(1,6)Glc, and the trisaccharide globotriose, Galα(1,4)Galβ(1,4)Glc. Recombinant MytiLec expressed in bacteria showed the same haemagglutinating and cytotoxic activity against Burkitt's lymphoma (Raji) cells as the native form. The crystal structure has been determined to atomic resolution, in the presence and absence of ligands, showing the protein to be a member of the β-trefoil family, but with a mode of ligand binding unique to a small group of related trefoil lectins. Each of the three pseudo-equivalent binding sites within the monomer shows ligand binding, and the protein forms a tight dimer in solution. An engineered monomer mutant lost all cytotoxic activity against Raji cells, but retained some haemagglutination activity, showing that the quaternary structure of the protein is important for its cellular effects.