6EKE
crystal structure of a Pholiota squarrosa lectin unliganded
Summary for 6EKE
| Entry DOI | 10.2210/pdb6eke/pdb |
| Descriptor | lectin, ZINC ION, ACETATE ION, ... (5 entities in total) |
| Functional Keywords | lectin, sugar binding protein |
| Biological source | Pholiota squarrosa |
| Total number of polymer chains | 3 |
| Total formula weight | 14877.28 |
| Authors | Cabanettes, A.,Varrot, A. (deposition date: 2017-09-26, release date: 2018-07-11, Last modification date: 2024-10-16) |
| 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
Download full validation report
