1iib

File:1iib.gif

spinqualitylabelsall models 1iib, resolution 1.8Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF IIBCELLOBIOSE FROM ESCHERICHIA COLI

OverviewOverview

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 StructureAbout 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].

ReferenceReference

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

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