1IIB

CRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLI

Summary for 1IIB

• Entry DOI: 10.2210/pdb1iib/pdb
• Descriptor: ENZYME IIB OF THE CELLOBIOSE-SPECIFIC PHOSPHOTRANSFERASE SYSTEM (2 entities in total)
• Functional Keywords: phosphoenolpyruvate dependent phosphotransferase system, iib enzymes, cysteine phosphorylation, phosphotransferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P69795
• Total number of polymer chains: 2
• Total formula weight: 22846.90

Authors

Van Montfort, R.L.M.,Pijning, T.,Kalk, K.H.,Reizer, J.,Saier, M.H.,Thunnissen, M.M.G.M.,Robillard, G.T.,Dijkstra, B.W. (deposition date: 1996-12-23, release date: 1997-12-24, Last modification date: 2024-02-07)

Primary citation

van Montfort, R.L.,Pijning, T.,Kalk, K.H.,Reizer, J.,Saier Jr., M.H.,Thunnissen, M.M.,Robillard, G.T.,Dijkstra, B.W.
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.
Structure, 5:217-225, 1997

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.

PubMed: 9032081
DOI: 10.1016/S0969-2126(97)00180-9

Experimental method

X-RAY DIFFRACTION (1.8 Å)