6a87

Pholiota squarrosa lectin (PhoSL) in complex with fucose(alpha1-6)GlcNAc

spinqualitylabelsall models 6a87, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6a87 is a 6 chain structure with sequence from Pholiota squarrosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.41Å Ligands: FUC, MEE, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A384E107_9AGAR Publication Abstract from PubMed Fucosylation of the N-glycan core via the alpha1-6 linkage (core fucosylation) is detected in specific types of cancers and related diseases, and thereby serves for a relevant biomarker. The lectin from a mushroom Pholiota squarrosa (PhoSL) shows a clear specificity to core fucosylation, without recognizing those with other types of fucosylation, such as the H type via the alpha1-2 linkage or the Lewis type via the alpha1-3 or alpha1-4 linkage. Here we determined the crystal structure of the PhoSL trimer in complex with a disaccharide fucose(alpha1-6)N-acetylglucosamine (GlcNAc). In the three sugar-binding pockets of PhoSL, extensive hydrophobic and hydrogen-bonding contacts were formed with the fucose moiety. In contrast, the GlcNAc moiety showed only a few hydrophobic and hydrogen-bonding contacts. To elucidate the mechanism for the specificity, we performed molecular dynamics simulations on this disaccharide and a trisaccharide fucose(alpha1-6)[GlcNAc(beta1-4)]GlcNAc in complex with PhoSL. It was observed that the GlcNAc corresponding to the outer one of the N-glycan core entered the sugar-binding pocket with the N-acetyl group placed stably at the bottom, forming extensive hydrophobic and hydrogen-bonding interactions. In addition, these glycans adopted unstressed favorable conformations when bound to PhoSL. In contrast, H- and Lewis-types of fucosylated trisaccharides adopting favorable conformations caused inevitable steric hindrance with the steep edge of the binding pocket, when docked with PhoSL. Therefore, the specificity to core fucosylation of PhoSL was achieved by a combination of these preferential and exclusive mechanisms. Structural basis for specific recognition of core fucosylation in N-glycans by Pholiota squarrosa lectin (PhoSL).,Yamasaki K, Kubota T, Yamasaki T, Nagashima I, Shimizu H, Terada RI, Nishigami H, Kang J, Taten M, Taten H Glycobiology. 2019 Mar 26. pii: 5420299. doi: 10.1093/glycob/cwz025. PMID:30913288 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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