Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2VUZ

Crystal structure of Codakine in complex with biantennary nonasaccharide at 1.7A resolution

Summary for 2VUZ
Entry DOI10.2210/pdb2vuz/pdb
Related2VUV
DescriptorCODAKINE, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
Functional Keywordsnonasaccharide, codakia orbicularis, sugar-binding protein, c-type, lectin, codakine, biantennary, invertebrate, sugar binding protein
Biological sourceCODAKIA ORBICULARIS
Total number of polymer chains1
Total formula weight15821.04
Authors
Gourdine, J.P.,Cioci, G.C.,Miguet, L.,Unverzagt, C.,Varrot, A.,Gauthier, C.,Smith-Ravin, E.J.,Imberty, A. (deposition date: 2008-06-02, release date: 2008-08-05, Last modification date: 2023-12-13)
Primary citationGourdine, J.P.,Cioci, G.C.,Miguet, L.,Unverzagt, C.,Silva, D.V.,Varrot, A.,Gautier, C.,Smith-Ravin, E.J.,Imberty, A.
High Affinity Interaction between a Bivalve C-Type Lectin and a Biantennary Complex-Type N-Glycan Revealed by Crystallography and Microcalorimetry.
J.Biol.Chem., 283:30112-, 2008
Cited by
PubMed Abstract: Codakine is an abundant 14-kDa mannose-binding C-type lectin isolated from the gills of the sea bivalve Codakia orbicularis. Binding studies using inhibition of hemagglutination indicated specificity for mannose and fucose monosaccharides. Further experiments using a glycan array demonstrated, however, a very fine specificity for N-linked biantennary complex-type glycans. An unusually high affinity was measured by titration microcalorimetry performed with a biantennary Asn-linked nonasaccharide. The crystal structure of the native lectin at 1.3A resolution revealed a new type of disulfide-bridged homodimer. Each monomer displays three intramolecular disulfide bridges and contains only one calcium ion located in the canonical binding site that is occupied by a glycerol molecule. The structure of the complex between Asn-linked nonasaccharide and codakine has been solved at 1.7A resolution. All residues could be located in the electron density map, except for the capping beta1-4-linked galactosides. The alpha1-6-linked mannose binds to calcium by coordinating the O3 and O4 hydroxyl groups. The GlcNAc moiety of the alpha1,6 arm engages in several hydrogen bonds with the protein, whereas the GlcNAc on the other antenna is stacked against Trp(108), forming an extended binding site. This is the first structural report for a bivalve lectin.
PubMed: 18687680
DOI: 10.1074/JBC.M804353200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon