Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N-acetylgalactosamine

• Published in: Proteins, structure, function, and bioinformatics structure, function, and bioinformatics, 2001-09, Vol.44 (4), p.470-478
• Main Authors: Rabijns, A., Verboven, C., Rougé, P., Barre, A., Van Damme, E.J.M., Peumans, W.J., De Ranter, C.J.
• Format: Article
• Language: English
• Subjects: Acacia - chemistry; Acetylglucosamine - chemistry; Acetylglucosamine - metabolism; Binding Sites; Crystallography, X-Ray; Hydrogen Bonding; Lectins - chemistry; Lectins - metabolism; legume lectin; Models, Molecular; Plant Lectins; Protein Binding; Protein Conformation; protein crystallography; Robinia pseudoacacia; RPbAI [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FNY]; RPbAI-Gal/NAc</ [http://www.rcsb.org/pdb/cgi/explore.cgi?pdbId=1FNZ]; Static Electricity; sugar-protein interactions; tetramer; Water - chemistry; Water - metabolism
• ISSN: 0887-3585; 1097-0134
• DOI: 10.1002/prot.1112

The structure of the bark lectin RPbAI (isoform A4) from Robinia pseudoacacia has been determined by protein crystallography both in the free form and complexed with N‐acetylgalactosamine. The free form is refined at 1.80 Å resolution to an R‐factor of 18.9% whereas the complexed structure has an R‐factor of 19.7% at 2.05 Å resolution. Both structures are compared to each other and to other available legume lectin structures. The polypeptide chains of the two structures exhibit the characteristic legume lectin tertiary fold. The quaternary structure resembles that of the Phaseolus vulgaris lectin, the soybean agglutinin, and the Dolichos biflorus lectin, but displays some unique features leading to the extreme stability of this lectin. Proteins 2001;44:470–478. © 2001 Wiley‐Liss, Inc.