PMID:9032081
| Citation |
van Montfort, RL, Pijning, T, Kalk, KH, Reizer, J, Saier, MH Jr, Thunnissen, MM, Robillard, GT and Dijkstra, BW (1997) The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases. Structure 5:217-25 |
|---|---|
| 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. |
| Links | |
| Keywords |
Animals; Bacterial Proteins/chemistry; Cattle; Crystallography, X-Ray; Eukaryotic Cells/enzymology; Models, Molecular; Oxidative Phosphorylation; Phosphoenolpyruvate Sugar Phosphotransferase System/chemistry; Protein Conformation; Protein Tyrosine Phosphatases/chemistry; Sequence Homology, Amino Acid |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.