5o7w

Crystal structure of the 4-FLUORO RSL lectin in complex with Lewis x tetrasaccharide

spinqualitylabelsall models 5o7w, resolution 1.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5o7w is a 2 chain structure with sequence from Ralstonia solanacearum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.35Å Ligands: 4FW, CA, EDO, FUC, GAL, GLA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0S4TLR1_RALSL Publication Abstract from PubMed Protein-carbohydrate interactions play crucial roles in biology. Understanding and modifying these interactions is of major interest for fighting many diseases. We took a synthetic biology approach and incorporated noncanonical amino acids into a bacterial lectin to modulate its interactions with carbohydrates. We focused on tryptophan, which is prevalent in carbohydrate binding sites. The exchange of the tryptophan residues with analogs fluorinated at different positions resulted in three distinctly fluorinated variants of the lectin from Ralstonia solanacearum. We observed differences in stability and affinity toward fucosylated glycans and rationalized them by X-ray and modeling studies. While fluorination decreased the aromaticity of the indole ring and, therefore, the strength of carbohydrate-aromatic interactions, additional weak hydrogen bonds were formed between fluorine and the ligand hydroxyl groups. Our approach opens new possibilities to engineer carbohydrate receptors. Effect of Noncanonical Amino Acids on Protein-Carbohydrate Interactions: Structure, Dynamics, and Carbohydrate Affinity of a Lectin Engineered with Fluorinated Tryptophan Analogs.,Tobola F, Lelimousin M, Varrot A, Gillon E, Darnhofer B, Blixt O, Birner-Gruenberger R, Imberty A, Wiltschi B ACS Chem Biol. 2018 Jun 12. doi: 10.1021/acschembio.8b00377. PMID:29812892 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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