Fig. 5: Crystal structure of SaroL-1. | Communications Biology

Fig. 5: Crystal structure of SaroL-1.

From: The choanoflagellate pore-forming lectin SaroL-1 punches holes in cancer cells by targeting the tumor-related glycosphingolipid Gb3

Fig. 5

a Cartoon representation of monomeric SaroL-1 in complex with GalNAc. β-trefoil-domain colored in blue and aerolysin domain in green. The GalNAc ligands are displayed in their electron density map as sticks. b Superimposition of β-trefoil lectin domains, (7QE4, light magenta), (7R55, blue) in complex with 3 molecules of GalNAc (violet) and 2 molecules of Gb3 (cyan). c Zoom on α, β and γ binding sites with GalNAc (violet) polar contacts are represented as dashed lines and bridging water molecules as red spheres. d Zoom on the interactions with Gb3 (cyan) in binding β and γ sites, polar contacts are represented as dashed lines and bridging water molecules as red spheres. e Overlay of β-trefoil domains of SaroL-1 (blue) in complex with Gb3 (cyan) and of monomeric CGL (5F90) (yellow) in complex with Gb3 and αGal1-4Gal (yellow). f Comparison of the structures of monomeric SaroL-1, pore-forming lectin LSL (1W3A) and ε-toxin (1UYJ) from left to right. The pro-aerolysin domain is colored in green and the membrane-binding domain in blue (SaroL-1), red (LSL) and orange (ε-toxin).

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