Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin
| Autor: | Hideharu Ishida, Makoto Kiso, Tatsuya Suzuki, Ryuichi Kato, Hisayoshi Makyio, Akihiro Imamura, Hiromune Ando, Junpei Shimabukuro |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Stereochemistry Aspergillus oryzae Biophysics Fucose binding Crystal structure Phase determination Crystallography X-Ray Biochemistry Fucose 03 medical and health sciences chemistry.chemical_compound Seleno-sugar Lectins Moiety Amino Acid Sequence Molecular Biology Binding Sites Sequence Homology Amino Acid biology Anomalous diffraction Lectin Cell Biology Carbohydrate biology.organism_classification 030104 developmental biology Affinity chemistry biology.protein |
| Zdroj: | Biochemical and Biophysical Research Communications. 477:477-482 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2016.06.069 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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