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5EO8

Crystal structure of AOL(868)

Summary for 5EO8
Entry DOI10.2210/pdb5eo8/pdb
Related5EO7
DescriptorPredicted protein, methyl 1-seleno-beta-L-fucopyranoside (3 entities in total)
Functional Keywordsseleno-fucoses, phaing, lectin, aspergillus oryzae, sugar binding protein
Biological sourceAspergillus oryzae RIB40 (Yellow koji mold)
Total number of polymer chains1
Total formula weight36022.50
Authors
Kato, R.,Kiso, M.,Ishida, H.,Ando, H.,Suzuki, T.,Shimabukuro, S.,Makyio, H. (deposition date: 2015-11-10, release date: 2016-06-29, Last modification date: 2024-03-20)
Primary citationMakyio, 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., 477:477-482, 2016
Cited by
PubMed 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.
PubMed: 27318092
DOI: 10.1016/j.bbrc.2016.06.069
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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数据于2024-10-30公开中

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