3WCR

Crystal structure of plant lectin (ligand-free form)

Summary for 3WCR

• Entry DOI: 10.2210/pdb3wcr/pdb
• Related: 3WCS 3WOG
• Descriptor: Erythroagglutinin, 2-acetamido-2-deoxy-beta-D-glucopyranose, BROMIDE ION, ... (4 entities in total)
• Functional Keywords: legume lectin fold, carbohydrate binding, n-glycan, sugar binding protein
• Biological source: Phaseolus vulgaris (Kidney bean)
• Total number of polymer chains: 2
• Total formula weight: 57200.16

Authors

Nagae, M.,Yamaguchi, Y. (deposition date: 2013-05-31, release date: 2014-04-09, Last modification date: 2024-10-16)

Primary citation

Nagae, M.,Soga, K.,Morita-Matsumoto, K.,Hanashima, S.,Ikeda, A.,Yamamoto, K.,Yamaguchi, Y.
Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold
Glycobiology, 24:368-378, 2014

PubMed 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 (Galβ1-4GlcNAcβ1-2Man) 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.

PubMed: 24436051
DOI: 10.1093/glycob/cwu004

Experimental method

X-RAY DIFFRACTION (2.45 Å)