Fig. 5

Ribbon representation of the RsDTE homology structure (a) and overview of the active site (b). The central β-strands and α-helices of TIM barrel-fold are shown in red and yellow, respectively. The additional α-helices are colored as green. The loops are colored as white. Catalytic residues are shown as yellow sticks. The substrate d-fructose is shown as green sticks. Mn(II) is displayed as a purple sphere. c Sequence alignment of RsDTE with from DTEs/DPEs from Rhodobacter aestuarii, Methanocaldococcus jannaschii, Rhodobacteraceae bacterium, Thermotoga maritime, Rhodobacter sphaeroides, Rhodobacter megalophilus, Rhodobacter sp. AKP1, Rhodobacter johrii, Pseudomonas cichorii, Clostridium cellulolyticum, Agrobacterium tumefaciens