1IUB

Fucose-specific lectin from Aleuria aurantia (Hg-derivative form)

Summary for 1IUB

• Entry DOI: 10.2210/pdb1iub/pdb
• Related: 1IUC
• Descriptor: Fucose-specific lectin, beta-L-fucopyranose, SULFATE ION, ... (6 entities in total)
• Functional Keywords: hg, mad, lectin, riken structural genomics/proteomics initiative, rsgi, structural genomics, sugar binding protein
• Biological source: Aleuria aurantia (orange peel mushroom)
• Total number of polymer chains: 1
• Total formula weight: 34322.44

Authors

Fujihashi, M.,Peapus, D.H.,Kamiya, N.,Nagata, Y.,Miki, K.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2002-03-01, release date: 2003-09-30, Last modification date: 2023-12-27)

Primary citation

Fujihashi, M.,Peapus, D.H.,Kamiya, N.,Nagata, Y.,Miki, K.
Crystal Structure of Fucose-Specific Lectin from Aleuria aurantia Binding Ligands at Three of Its Five Sugar Recognition Sites
Biochemistry, 42:11093-11099, 2003

PubMed Abstract: Aleuria aurantia possesses a fucose-specific lectin (AAL) that is widely used as a specific probe for fucose. Fucosylated sugars often play pivotal roles in many cellular processes. We have determined the crystal structure of AAL at 2.24 A resolution in complex with only three fucose molecules in its five sugar binding sites of a six-fold beta-propeller structure. Very recently, the structure of AAL has been independently determined, showing that all the five binding sites were occupied by fucose molecules [Wimmerova, M., et al. (2003) J. Biol. Chem. 278, 27059-27067]. Stabilization of the arginine conformation bound to fucose molecules plays an essential role in generating the difference in the affinity in the five binding sites. Binding models with a couple of saccharides based on biochemical assays suggest that hydrophobic contacts also play important roles in AAL recognizing its ligand.

PubMed: 14503859
DOI: 10.1021/bi034983z

Experimental method

X-RAY DIFFRACTION (2.31 Å)