The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.
van Montfort, R.L., Pijning, T., Kalk, K.H., Reizer, J., Saier Jr., M.H., Thunnissen, M.M., Robillard, G.T., Dijkstra, B.W.(1997) Structure 5: 217-225
- PubMed: 9032081 
- DOI: https://doi.org/10.1016/s0969-2126(97)00180-9
- Primary Citation of Related Structures:  
1IIB - PubMed Abstract: 
. The bacterial phosphoenolpyruvate-dependent phosphotransferase system (PTS) mediates the energy-driven uptake of carbohydrates and their concomitant phosphorylation. In addition, the PTS is intimately involved in the regulation of a variety of metabolic and transcriptional processes in the bacterium. The multiprotein PTS consists of a membrane channel and at least four cytoplasmic proteins or protein domains that sequentially transfer a phosphoryl group from phosphoenolpyruvate to the transported carbohydrate. Determination of the three-dimensional structure of the IIB enzymes within the multiprotein complex would provide insights into the mechanisms by which they promote efficient transport by the membrane channel IIC protein and phosphorylate the transported carbohydrate on the inside of the cell.
Organizational Affiliation: 
Laboratory of Biophysical Chemistry, Biochemistry and BIOSON Research Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen The Netherlands.