1axy

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1axy, resolution 1.95Å

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ERYTHRINA CORALLODENDRON LECTIN

Overview

The structures of the Erythrina corallodendron lectin (EcorL) and of its, complexes with galactose, N-acetylgalactosamine, lactose and, N-acetyllactosamine were determined at a resolution of 1.9 to 1.95 A. The, final R-values of the five models are in the range 0.169 to 0.181. The, unusual, non-canonical, dimer interface of EcorL is made of beta-strands, from the two monomers, which face one another in a "hand-shake" mode. The, galactose molecule in the primary binding site is bound in an identical, way in all four complexes. Features of the electrostatic potential of the, galactose molecule match those of the potential in the combining site, thus probably pointing to the contribution of the electrostatic energy to, determining the orientation of the ligand. No conformational change occurs, in the protein upon binding the ligand. Subtle variations in the binding, mode of the second monosaccharide (glucose in the complex with lactose and, N-acetylglucosamine in the complex with N-acetyllactosamine) were, observed. The mobility of Gln219 is lower in the complexes with the, disaccharides than in the complexes with the monosaccharides, indicating, further recruitment of this residue to ligand binding through more, extensive hydrogen bonding in the former complexes. Water molecules that, have been located in the combining sites of the five structures undergo, rearrangement in response to binding of the different ligands. The new, structural information is in qualitative agreement with thermodynamic data, on the binding to EcorL.

About this Structure

1AXY is a Single protein structure of sequence from Erythrina corallodendron with MN and CA as ligands. Full crystallographic information is available from OCA.

Reference

Structures of the Erythrina corallodendron lectin and of its complexes with mono- and disaccharides., Elgavish S, Shaanan B, J Mol Biol. 1998 Apr 10;277(4):917-32. PMID:9545381

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