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![[Figure 3]](ji5024fig3mag.jpg)
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Figure 3
The structure of the active site in EbBcsZ(D242A)CPT. (a) Electron densities of the β-1,4-glucan chains bound to the four monomers of the asymmetric unit. The electron densities are the omit map contoured at 3.0σ. (b) Interactions between the β-1,4-glucan chains and the residues in the active site. We selected monomer A as the representative active site. The water molecules and the residues interacting with the β-1,4-glucan chains are represented as red spheres and light blue lines, respectively. The hydrogen-bond network is represented as dotted lines. In (a) and (b), the β-1,4-glucan chains are shown as sticks and O, N and C atoms are shown in red, blue and dark cyan, respectively. (c) The conformation of G−1 (dark cyan) and five other glucosyl units in subsites G−2, G−3, G−4, G+1 and G+2 (light gray) of EbBcsZ(D242A)CPT. (d) Superposed views of glucosyl units. Left: superposition of G−1 (dark cyan) and G−2 (light gray) in EbBcsZ(D242A)CPT. Right: superposition of G−1 in EbBcsZ(D242A)CPT (dark cyan) and G−1 in CtCelA(E95Q)CPT (yellow). |
![[Figure 3]](ji5024fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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