Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10748066 | Biochemical and Biophysical Research Communications | 2016 | 6 Pages |
Abstract
The crystal structure of AOL (a fucose-specific lectin of Aspergillus oryzae) has been solved by SAD (single-wavelength anomalous diffraction) and MAD (multi-wavelength anomalous diffraction) phasing of seleno-fucosides. The overall structure is a six-bladed β-propeller similar to that of other fucose-specific lectins. The fucose moieties of the seleno-fucosides are located in six fucose-binding sites. Although the Arg and Glu/Gln residues bound to the fucose moiety are common to all fucose-binding sites, the amino-acid residues involved in fucose binding at each site are not identical. The varying peak heights of the seleniums in the electron density map suggest that each fucose-binding site has a different carbohydrate binding affinity.
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Authors
Hisayoshi Makyio, Junpei Shimabukuro, Tatsuya Suzuki, Akihiro Imamura, Hideharu Ishida, Makoto Kiso, Hiromune Ando, Ryuichi Kato,