Extended Data Fig. 3: Structural alignment of human FUT9 with H. pylori FucT. | Nature Chemical Biology

Extended Data Fig. 3: Structural alignment of human FUT9 with H. pylori FucT.

From: Structural basis for Lewis antigen synthesis by the α1,3-fucosyltransferase FUT9

Extended Data Fig. 3: Structural alignment of human FUT9 with H. pylori FucT.The alternative text for this image may have been generated using AI.

(a, b) Structure of FUT9:GDP-CF3-Fuc:H-type 2 (green cartoon for protein, white and yellow sticks for the donor and H-type 2, respectively) and (c, d) HpFucT:GDP-Fuc complex (PDB 2NZY29, orange cartoon for protein and cyan sticks for GDP-Fuc) were (e, f) aligned based on structural similarity of the donor binding domain. (g) A zoom in view of the aligned structures are highlighted for the donor binding site (red box) and the acceptor binding site (blue box). (h) The donor binding site is further displayed with interacting residues shown as thin sticks (FUT9 as green sticks and HpFucT as orange sticks) and the GDP-CF3-Fuc as white sticks and GDP-Fuc as cyan sticks). (i) The acceptor binding site is further displayed with interacting residues shown as thin sticks colored as in panel h. The H-type 2 acceptor structure is shown as yellow sticks.

Back to article page