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J. Biol. Chem., Vol. 278, Issue 29, 27059-27067, July 18, 2003

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Crystal Structure of Fungal Lectin

SIX-BLADED -PROPELLER FOLD AND NOVEL FUCOSE RECOGNITION MODE FOR ALEURIA AURANTIA LECTIN^*

Michaela Wimmerova   ¶, Edward Mitchell ¶ ||, Jean-Frederic Sanchez ** , Catherine Gautier ** and Anne Imberty ** 

From the National Centre for Biomolecular Research and Department of Biochemistry, Masaryk University, 611 37 Brno, Czech Republic, ^||European Synchroton Radiation Facility Experiments Division, BP 220, F-38043 Grenoble cedex, France, and ^**Centre de Recherches sur les Macromolécules Végétales-CNRS (affiliated with Université Joseph Fourier), BP 53, F-38041 Grenoble cedex 09, France

Aleuria aurantia lectin is a fungal protein composed of two identical 312-amino acid subunits that specifically recognizes fucosylated glycans. The crystal structure of the lectin complexed with fucose reveals that each monomer consists of a six-bladed -propeller fold and of a small antiparallel two-stranded -sheet that plays a role in dimerization. Five fucose residues were located in binding pockets between the adjacent propeller blades. Due to repeats in the amino acid sequence, there are strong similarities between the sites. Oxygen atoms O-3, O-4, and O-5 of fucose are involved in hydrogen bonds with side chains of amino acids conserved in all repeats, whereas O-1 and O-2 interact with a large number of water molecules. The nonpolar face of each fucose residue is stacked against the aromatic ring of a Trp or Tyr amino acid, and the methyl group is located in a highly hydrophobic pocket. Depending on the precise binding site geometry, the - or -anomer of the fucose ligand is observed bound in the crystal. Surface plasmon resonance experiments conducted on a series of oligosaccharides confirm the broad specificity of the lectin, with a slight preference for Fuc1–2Gal disaccharide. This multivalent carbohydrate recognition fold is a new prototype of lectins that is proposed to be involved in the host recognition strategy of several pathogenic organisms including not only the fungi Aspergillus but also the phytopathogenic bacterium Ralstonia solanacearum.

Received for publication, March 14, 2003 , and in revised form, April 28, 2003.

The atomic coordinates and structure factors (code 1OFZ) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

^* Travels and visits between the National Center for Biomolecular Research and Centre de Recherches sur les Macromolécules Végétales are supported by a BARRANDE exchange program. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Stay in Grenoble supported by the French minister program for invited scientists and partial financial support from the Ministry of Education of the Czech Republic by Grant LN00A016.

^¶ These two authors contributed equally to this work.

Supported by a grant from the French association La Ligue Contre le Cancer.

To whom correspondence should be addressed. Tel.: 33-476-03-76-36; Fax: 33-476-54-72-03; E-mail: imberty{at}cermav.cnrs.fr.

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