3WOG: Crystal structure plant lectin in complex with ligand

Citation:
Abstract
Phytohemagglutinin from Phaseolus vulgaris (PHA-E), a legume lectin, has an unusual specificity toward biantennary galactosylated N-glycan with bisecting N-acetylglucosamine (GlcNAc). To investigate the interaction in detail, we have solved the crystal structures of PHA-E without ligand and in complex with biantennary N-glycan derivatives. PHA-E interacts with the trisaccharide unit (Galbeta1-4GlcNAcbeta1-2Man) in a manner completely different from that of mannose/glucose-specific legume lectins. The inner mannose residue binds to a novel site on the protein, and its rotation is opposite to that occurring in the monosaccharide-binding site of other lectins around the sugar O3 axis. Saturation-transfer difference NMR using biantennary di-galactosylated and bisected glycans reveals that PHA-E interacts with both antennas almost equally. The unique carbohydrate interaction explains the glycan-binding specificity and high affinity.
PDB ID: 3WOGDownload
MMDB ID: 118960
PDB Deposition Date: 2013/12/26
Updated in MMDB: 2017/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 3WOG: tetrameric; determined by author and by software (PISA)
Molecular Components in 3WOG
Label Count Molecule
Proteins (4 molecules)
4
Erythroagglutinin
Molecule annotation
Chemicals (20 molecules)
1
8
2
4
3
4
4
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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