In two separate studies at the Advanced Photon Source, researchers used high-resolution synchrotron protein crystallography to determine the crystal structures of ROK (bacterial Repressors, uncharacterized Open reading frames, and sugar Kinases) fructokinase from Bacillus subtilis and a recombinant a-glucosidase from the human gut bacterium Ruminococcus obeum. The results provided new information about how enzymes bind, recognize, and process carbohydrate substrates and how variations in enzyme structure impact enzyme function. These findings are expected to improve the conversion of biomass to fuels by using structural information to optimize enzymes for bioprocessing.
References: Nocek, B., et al. 2011. “Structural Studies of ROK Fructokinase YdhR from Bacillus subtilis: Insights into Substrate Binding and Fructose Specificity,” Journal of Molecular Biology 406, 325–42.
Tan, K., et al. 2010. “Novel a-Glucosidase from Human Gut Microbiome: Substrate Specificities and Their Switch,” The FASEB Journal 24, 3939–49.
SC-23.2 Biological Systems Science Division, BER
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