1FAY

WINGED BEAN ACIDIC LECTIN COMPLEXED WITH METHYL-ALPHA-D-GALACTOSE (MONOCLINIC FORM)

Summary for 1FAY

• Entry DOI: 10.2210/pdb1fay/pdb
• Related: 1F9K
• Descriptor: ACIDIC LECTIN, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, methyl alpha-D-galactopyranoside, ... (6 entities in total)
• Functional Keywords: legume lectin, glycosylated protein, h-antigenic specificity, agglutinin, sugar binding protein
• Biological source: Psophocarpus tetragonolobus (winged bean)
• Total number of polymer chains: 8
• Total formula weight: 215980.97

Authors

Manoj, N.,Srinivas, V.R.,Surolia, A.,Vijayan, M.,Suguna, K. (deposition date: 2000-07-14, release date: 2001-07-14, Last modification date: 2024-10-30)

Primary citation

Manoj, N.,Srinivas, V.R.,Surolia, A.,Vijayan, M.,Suguna, K.
Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin.
J.Mol.Biol., 302:1129-1137, 2000

PubMed Abstract: Structures of two crystal forms of the dimeric acidic winged bean agglutinin (WBAII) complexed with methyl-alpha-D-galactose have been determined at 3.0 A and 3.3 A resolution. The subunit structure and dimerisation of the lectin are similar to those of the basic lectin from winged bean (WBAI) and the lectin from Erythrina corallodendron (EcorL). The conformation of a loop and its orientation with respect to the rest of the molecule in WBAII are, however, different from those in all the other legume lectins of known structure. This difference appears to have been caused by the formation of two strategically placed salt bridges in the former. Modelling based on the crystal structures provides a rationale for the specificity of the lectin, which is very different from that of WBAI, for the H-antigenic determinant responsible for O blood group reactivity. It also leads to a qualitative explanation for the thermodynamic data on sugar-binding to the lectin, with special emphasis on the role of a tyrosyl residue in the variable loop in the sugar-binding region in generating the carbohydrate specificity of WBAII.

PubMed: 11183779
DOI: 10.1006/jmbi.2000.4111

Experimental method

X-RAY DIFFRACTION (3.3 Å)