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. 2021 Jun 28;60(27):2206–2220. doi: 10.1021/acs.biochem.1c00305

Figure 2.

Figure 2

Overall fold and binding site of CBM9.3 in comparison to those of TmCBM9-2. (A) CBM9.3 with the binding sites Tyr89 (top residue) and Trp191 (bottom residue) shown as green sticks. The C-terminal “tail” formed by linker residues is seen on the right side of the protein. (B) TmCBM9-2 (PDB entry 1I8U) with binding sites Trp71 (top residue) and Trp175 (bottom residue) shown as cyan sticks. Calcium atoms are shown as black spheres. Close-ups of the binding sites of (C) CBM9.3 and (D) TmCBM9-2 (with cellobiose bound), with the former having the binding residues in an open groove that in the latter is blocked on one end. Residues blocking the binding groove in TmCBM9-2 are colored red in panel D, with equivalently positioned residues in CBM9.3 also colored red in panel C. The blockage of the groove by these residues is shown using mesh.