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![[Figure 4]](ji5024fig4mag.jpg)
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Figure 4
The structure of the secondary binding site in EbBcsZ(D242A)CPT. (a) Close-up view of the secondary binding site. The cellotriose and the residues interacting with it are represented as sticks and lines, respectively. The hydrogen bonds between cellotriose and the residues of EbBcsZ(D242A)CPT are represented as dotted lines. (b) Superposition of the residues interacting with cellotriose in EbBcsZ and the other endo-β-1,4-glucanases. The residues of EbBcsZ(D242A)CPT (dark cyan), EcBcsZ(E55Q)CPT (PDB entry 3qxq, orange), CMCax (PDB entry 1wzz, pink), Cel10 (PDB entry 5gy3, blue), BcsZ (PDB entry 4q2b, gray) and hydrolase from Vibrio fischeri (PDB entry 5cd2, yellow) are labeled and represented as lines. The β-hairpin region of EbBcsZ(D242A)CPT and the corresponding regions in the other endo-β-1,4-glucanases are represented as ribbons. |
![[Figure 4]](ji5024fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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