6FX3
crystal structure of Pholiota squarrosa lectin in complex with a dodecasaccharide
Summary for 6FX3
| Entry DOI | 10.2210/pdb6fx3/pdb |
| Descriptor | lectin, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]1-azido-beta-N-acetyl-D-glucosamine, N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]1-azido-beta-N-acetyl-D-glucosamine, ... (4 entities in total) |
| Functional Keywords | lectin, dodecasaccharide, sugar binding protein |
| Biological source | Pholiota squarrosa |
| Total number of polymer chains | 2 |
| Total formula weight | 12940.72 |
| Authors | Cabanettes, A.,Varrot, A. (deposition date: 2018-03-08, release date: 2018-07-11, Last modification date: 2024-05-01) |
| Primary citation | Cabanettes, A.,Perkams, L.,Spies, C.,Unverzagt, C.,Varrot, A. Recognition of Complex Core-Fucosylated N-Glycans by a Mini Lectin. Angew. Chem. Int. Ed. Engl., 57:10178-10181, 2018 Cited by PubMed Abstract: The mini fungal lectin PhoSL was recombinantly produced and characterized. Despite a length of only 40 amino acids, PhoSL exclusively recognizes N-glycans with α1,6-linked fucose. Core fucosylation influences the intrinsic properties and bioactivities of mammalian N-glycoproteins and its level is linked to various cancers. Thus, PhoSL serves as a promising tool for glycoprofiling. Without structural precedence, the crystal structure was solved using the zinc anomalous signal, and revealed an interlaced trimer creating a novel protein fold termed β-prism III. Three biantennary core-fucosylated N-glycan azides of 8 to 12 sugars were cocrystallized with PhoSL. The resulting highly resolved structures gave a detailed view on how the exclusive recognition of α1,6-fucosylated N-glycans by such a small protein occurs. This work also provided a protein consensus motif for the observed specificity as well as a glimpse into N-glycan flexibility upon binding. PubMed: 29956878DOI: 10.1002/anie.201805165 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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