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. 2014 Sep 11;10(9):e1004364. doi: 10.1371/journal.ppat.1004364

Figure 5. Structures of the CBM71 modules in BgaA.

Figure 5

(A) A cartoon representation of CBM71-1 in complex with LacNAc. The protein is color ramped red to blue from the N-terminus to the C-terminus. A bound calcium atom is shown in magenta. The binding site of the CBM is shown as a grey transparent surface with the bound LacNAc molecule shown as green stick. The electron density for the LacNAc is shown as a blue-mesh F o-F c maximum-likelihood/σA-weighted map contoured at 3σ (0.33 e−/Å3). (B) An overlap of the structure of CBM71-2 (purple) with CBM71-1 (grey). The LacNAc molecule bound to CBM71-1 is shown as green sticks. (C) Expanded view of the CBM71 binding site shown in divergent stereo. CBM71-1 is shown in grey with the LacNAc shown as green sticks, residues involved in binding the LacNAc as grey sticks, and the interacting water network as red spheres. Black dashed lines represent potential hydrogen bonds. CBM71-2 is shown in purple; residues conserved with CBM71-2 are shown as purple sticks. (D) An overlap of the CBM71-1 LacNAc complex (grey with LacNAc in green) with the CBM32 from C. perfringens NagJ (blue with bound LacNAc shown as blue sticks).