Structural highlights
Publication Abstract from PubMed
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 beta-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.
Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin.,Makyio H, Shimabukuro J, Suzuki T, Imamura A, Ishida H, Kiso M, Ando H, Kato R Biochem Biophys Res Commun. 2016 Jun 16. pii: S0006-291X(16)30987-1. doi:, 10.1016/j.bbrc.2016.06.069. PMID:27318092[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Makyio H, Shimabukuro J, Suzuki T, Imamura A, Ishida H, Kiso M, Ando H, Kato R. Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin. Biochem Biophys Res Commun. 2016 Jun 16. pii: S0006-291X(16)30987-1. doi:, 10.1016/j.bbrc.2016.06.069. PMID:27318092 doi:http://dx.doi.org/10.1016/j.bbrc.2016.06.069
