6zu2 | pdb_00006zu2

CML1 crystal structure in complex with H-type 1 trisaccharide

spinqualitylabelsall models 6zu2, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zu2 is a 6 chain structure with sequence from Coprinopsis cinerea. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.55Å Ligands: FUC, GAL, NAG, PRD_900049, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B3VS76_COPCI Publication Abstract from PubMed Lectins are non-immunoglobulin-type proteins that bind to specific carbohydrate epitopes and play important roles in intra- and inter-organismic interactions. Here, we describe a novel fucose-specific lectin, termed CML1, which we identified from fruiting body extracts of Coprinopsis cinerea. For further characterization, the coding sequence for CML1 was cloned and heterologously expressed in Escherichia coli. Feeding of CML1-producing bacteria inhibited larval development of the bacterivorous nematode Caenorhabditis tropicalis, but not of C. elegans. The crystal structure of the recombinant protein in its apo-form and in complex with H type I or Lewis A blood group antigens was determined by X-ray crystallography. The protein folds as a sandwich of two antiparallel beta-sheets and forms hexamers resulting from a trimer of dimers. The hexameric arrangement was confirmed by small-angle scattering of X-rays (SAXS). One carbohydrate binding site per protomer was found at the dimer interface with both protomers contributing to ligand binding, resulting in a hexavalent lectin. In terms of lectin activity of recombinant CML1, substitution of the carbohydrate-interacting residues His54, Asn55, Trp94 and Arg114 by Ala abolished carbohydrate-binding and nematotoxicity. While no similarities to any characterized lectin were found, sequence alignments identified many non-characterized agaricomycete proteins. These results suggest that CML1 is the founding member of a novel family of fucoside-binding lectins involved in the defense of agaricomycete fruiting bodies against predation by fungivorous nematodes. Structure-function relationship of a novel fucoside-binding fruiting body lectin from Coprinopsis cinerea exhibiting nematotoxic activity.,Bleuler-Martinez S, Varrot A, Olieric V, Schubert M, Vogt E, Fetz C, Wohlschlager T, Plaza DF, Walti M, Duport Y, Capitani G, Aebi M, Kunzler M Glycobiology. 2022 Mar 22. pii: 6551971. doi: 10.1093/glycob/cwac020. PMID:35323921 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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