Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin
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. - Highlights: • The six-bladed β-propeller structure of AOL was solved by seleno-sugar phasing. • The mode of fucose binding is essentially conserved at all six binding sites. • The seleno-fucosides exhibit slightly different interactions and electron densities. • These findings suggest that the affinity for fucose is not identical at each site.
- Authors:
-
- Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), 1-1 Oho, Tsukuba, Ibaraki, 305-0801 (Japan)
- Department of Applied Bioorganic Chemistry, Gifu University, 1-1 Yanagido, Gifu-shi, Gifu 501-1193 (Japan)
- Publication Date:
- OSTI Identifier:
- 22606172
- Resource Type:
- Journal Article
- Journal Name:
- Biochemical and Biophysical Research Communications
- Additional Journal Information:
- Journal Volume: 477; Journal Issue: 3; Other Information: Copyright (c) 2016 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; 60 APPLIED LIFE SCIENCES; AFFINITY; AMINO ACIDS; ASPERGILLUS; CRYSTAL STRUCTURE; CRYSTALS; DIFFRACTION; ELECTRON DENSITY; HEXOSES; LECTINS; RICE; SACCHAROSE; SELENIUM; WAVELENGTHS
Citation Formats
Makyio, Hisayoshi, Shimabukuro, Junpei, Suzuki, Tatsuya, Institute for Integrated Cell-Material Sciences, Imamura, Akihiro, Ishida, Hideharu, Kiso, Makoto, Institute for Integrated Cell-Material Sciences, Ando, Hiromune, Institute for Integrated Cell-Material Sciences, and Kato, Ryuichi. Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin. United States: N. p., 2016.
Web. doi:10.1016/J.BBRC.2016.06.069.
Makyio, Hisayoshi, Shimabukuro, Junpei, Suzuki, Tatsuya, Institute for Integrated Cell-Material Sciences, Imamura, Akihiro, Ishida, Hideharu, Kiso, Makoto, Institute for Integrated Cell-Material Sciences, Ando, Hiromune, Institute for Integrated Cell-Material Sciences, & Kato, Ryuichi. Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin. United States. https://doi.org/10.1016/J.BBRC.2016.06.069
Makyio, Hisayoshi, Shimabukuro, Junpei, Suzuki, Tatsuya, Institute for Integrated Cell-Material Sciences, Imamura, Akihiro, Ishida, Hideharu, Kiso, Makoto, Institute for Integrated Cell-Material Sciences, Ando, Hiromune, Institute for Integrated Cell-Material Sciences, and Kato, Ryuichi. 2016.
"Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin". United States. https://doi.org/10.1016/J.BBRC.2016.06.069.
@article{osti_22606172,
title = {Six independent fucose-binding sites in the crystal structure of Aspergillus oryzae lectin},
author = {Makyio, Hisayoshi and Shimabukuro, Junpei and Suzuki, Tatsuya and Institute for Integrated Cell-Material Sciences and Imamura, Akihiro and Ishida, Hideharu and Kiso, Makoto and Institute for Integrated Cell-Material Sciences and Ando, Hiromune and Institute for Integrated Cell-Material Sciences and Kato, Ryuichi},
abstractNote = {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. - Highlights: • The six-bladed β-propeller structure of AOL was solved by seleno-sugar phasing. • The mode of fucose binding is essentially conserved at all six binding sites. • The seleno-fucosides exhibit slightly different interactions and electron densities. • These findings suggest that the affinity for fucose is not identical at each site.},
doi = {10.1016/J.BBRC.2016.06.069},
url = {https://www.osti.gov/biblio/22606172},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 477,
place = {United States},
year = {Fri Aug 26 00:00:00 EDT 2016},
month = {Fri Aug 26 00:00:00 EDT 2016}
}