6jk3

Crystal structure of a mini fungal lectin, PhoSL in complex with core-fucosylated chitobioseCrystal structure of a mini fungal lectin, PhoSL in complex with core-fucosylated chitobiose

Structural highlights 6jk3 is a 3 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 1.12Å Ligands: , , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A3B6UEU4_9AGAR Publication Abstract from PubMed PhoSL (Pholiota squarrosa Lectin) has an exceptional binding affinity for biomolecules with core-fucosylated N-glycans. This modification involves the addition of fucose to the inner N-acetylglucosamine within the N-glycan structure and is known to influence many physiological processes. Nevertheless, the molecular interactions underlying high-affinity binding of native PhoSL to core-fucosylated N-glycans remain largely unknown. In this study, we devised a strategy to produce PhoSL with the essential structural characteristics of the native protein (n-PhoSL). To do so, a fusion protein was expressed in E. coli and purified. Then, enzymatic cleavage and incubation with glutathione were utilized to recapitulate the native primary structure and disulfide bonding pattern. Subsequently, we identified the residues crucial for n-PhoSL binding to core-fucosylated chitobiose (N2F) via NMR spectroscopy. Additionally, crystal structures were solved for both apo n-PhoSL and its N2F complex. These analyses suggested a pivotal role of the N-terminal amine in maintaining the integrity of the binding pocket and actively contributing to core-fucose recognition. In support of this idea, the inclusion of additional residues at the N-terminus considerably reduced binding affinity and PhoSL cytotoxicity toward breast cancer cells. Taken together, these findings can facilitate the utilization of PhoSL in basic research, diagnostics and therapeutic strategies. Structural insights into the role of N-terminal integrity in PhoSL for core-fucosylated N-glycan recognition.,Lou YC, Tu CF, Chou CC, Yeh HH, Chien CY, Sadotra S, Chen C, Yang RB, Hsu CH Int J Biol Macromol. 2024 Jan;255:128309. doi: 10.1016/j.ijbiomac.2023.128309. , Epub 2023 Nov 21. PMID:37995778 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 6jk3, resolution 1.12Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image