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1iib
From Proteopedia
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CRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLI
Overview
BACKGROUND:. 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 ... [(full description)]
About this Structure
1IIB is a [Single protein] structure of sequence from [Escherichia coli]. Active as [Protein-N(pi)-phosphohistidine--sugar phosphotransferase], with EC number [2.7.1.69]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
Reference
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases., van Montfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Thunnissen MM, Robillard GT, Dijkstra BW, Structure. 1997 Feb 15;5(2):217-25. PMID:9032081
Page seeded by OCA on Tue Oct 30 15:39:32 2007
Categories: Escherichia coli | Protein-N(pi)-phosphohistidine--sugar phosphotransferase | Single protein | Dijkstra, B.W. | Kalk, K.H. | Montfort, R.L.M.Van. | Pijning, T. | Reizer, J. | Robillard, G.T. | Saier, M.H. | Thunnissen, M.M.G.M. | Cysteine phosphorylation | Iib enzymes | Phosphoenolpyruvate dependent phosphotransferase system | Phosphotransferase
