Escherichia coli arabinose-binding protein

Fig. 21. Stereodrawing of L-arabinose bound to L-arabinose-binding protein from Escherichia coli. The edge-to-face interaction between tryptophan-16 and phenylalanine-17 gives rise to a hydrophobic surface that interacts with the hydrophobic portion of the sugar. Reproduced with permission from Quiocho and Vyas (1984).

Fig. 1 Crystal structures of the periplasmic L-arabinose-binding protein (ABP) of Escherichia coli complexed to a-L-arabinose (left. PDB entry lABE) and of galectin-1 complexed to A-acetyllactosamine (right, PDB entry ISLT). (From Refs. [13-15]). (View this art in color at www.dekker.com.)...

The L-arabinose-binding protein from Escherichia coli also shows two domains with a cleft between them. Quiocho et in this case too, comment on the similarities between the secondary-structural features of these domains, each... 

Ogden, S., Haggety, D., Stoner, C. M., Kolodrubetz, D., and Schleif, R. (1980). The Escherichia coli L-arabinose operon binding sites of the regulatory proteins and a mechanism of positive and negative regulation. Proc. Nat. Acad. Sci. USA 77,3346-3350. 

Initially, the detection of environmental signals occurred inside cells. Chemicals that could pass into cells, either by diffusion through the cell membrane or by the action of transport proteins, and could bind directly to proteins inside the cell and modulate their activities. An example is the use of the sugar arabinose by the bacterium Escherichia coli (Figure 2.19). E. coli cells are normally unable to use arabinose efficiently as a source of... 

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