Fig. 5
From: Determination of the native features of the exoglucanase Cel48S from Clostridium thermocellum
Structural analysis of ctCel48S_CD from C. thermocellum DSM1313. a The overall structure of ctCel48S_CD in complexation with PEG. The core (α/α)6 barrels are colored in orange, the additional α-helixes in slate, and β-sheets in pink. b The substrate-binding tunnel of ctCel48S_CD with a bound PEG. PEG is in cyan, and residues that distribute in the catalytic tunnel are shown in blue sticks. The 2F o F c densities for PEG and residues are contoured in blue in 1.0σ. c Superimposed structures of ctCel48S_CD and rCel48S_CD. The rCel48S_CD structure (1L2A) is in blue, and the oligosaccharides are in yellow. The ctCel48S_CD is in orange, and the bound PEG is in cyan. d Superposition of the residues responsible for substrate binding and catalysis. Residues of rCel48S_CD and ctCel48S_CD are in blue and orange, respectively. e The analysis of the conformationals change of residues in the catalytic center. The oligosaccharides are in yellow. The rCel48S_CD and ctCel48S_CD structures are in blue and orange, respectively. The possible hydrogen bonds are represented by dash line, and the distances are shown in angstroms