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

1BJQ

THE DOLICHOS BIFLORUS SEED LECTIN IN COMPLEX WITH ADENINE

Summary for 1BJQ
Entry DOI10.2210/pdb1bjq/pdb
DescriptorLECTIN, CALCIUM ION, MANGANESE (II) ION, ... (4 entities in total)
Functional Keywordsglycoprotein, lectin, adenine, quaternary structure, legume lectin
Biological sourceVigna unguiculata subsp. cylindrica (horse gram)
Total number of polymer chains8
Total formula weight218761.77
Authors
Hamelryck, T.W.,Loris, R.,Bouckaert, J.,Dao-Thi, M.H.,Wyns, L.,Etzler, M. (deposition date: 1998-06-26, release date: 1998-12-30, Last modification date: 2024-05-22)
Primary citationHamelryck, T.W.,Loris, R.,Bouckaert, J.,Dao-Thi, M.H.,Strecker, G.,Imberty, A.,Fernandez, E.,Wyns, L.,Etzler, M.E.
Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus.
J.Mol.Biol., 286:1161-1177, 1999
Cited by
PubMed Abstract: The seed lectin (DBL) from the leguminous plant Dolichos biflorus has a unique specificity among the members of the legume lectin family because of its high preference for GalNAc over Gal. In addition, precipitation of blood group A+H substance by DBL is slightly better inhibited by a blood group A trisaccharide (GalNAc(alpha1-3)[Fuc(alpha1-2)]Gal) containing pentasaccharide, and about 40 times better by the Forssman disaccharide (GalNAc(alpha1-3)GalNAc) than by GalNAc. We report the crystal structures of the DBL-blood group A trisaccharide complex and the DBL-Forssman disaccharide complex.A comparison with the binding sites of Gal-binding legume lectins indicates that the low affinity of DBL for Gal is due to the substitution of a conserved aromatic residue by an aliphatic residue (Leu127). Binding studies with a Leu127Phe mutant corroborate these conclusions. DBL has a higher affinity for GalNAc because the N-acetyl group compensates for the loss of aromatic stacking in DBL by making a hydrogen bond with the backbone amide group of Gly103 and a hydrophobic contact with the side-chains of Trp132 and Tyr104. Some legume lectins possess a hydrophobic binding site that binds adenine and adenine-derived plant hormones, i.e. cytokinins. The exact function of this binding site is unknown, but adenine/cytokinin-binding legume lectins might be involved in storage of plant hormones or plant growth regulation. The structures of DBL in complex with adenine and of the dimeric stem and leaf lectin (DB58) from the same plant provide the first structural data on these binding sites. Both oligomers possess an unusual architecture, featuring an alpha-helix sandwiched between two monomers. In both oligomers, this alpha-helix is directly involved in the formation of the hydrophobic binding site. DB58 adopts a novel quaternary structure, related to the quaternary structure of the DBL heterotetramer, and brings the number of know legume lectin dimer types to four.
PubMed: 10047489
DOI: 10.1006/jmbi.1998.2534
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

229380

数据于2024-12-25公开中

PDB statisticsPDBj update infoContact PDBjnumon