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Like an opera house, which has its public entranceseparate from that for the performers, a cell hasdifferent doors for different molecules. Each getsscrutinized at its door before it can enter the cell.Now researchers from the University of California atSan Francisco have revealed in the journal Science the three-dimensional structure of one suchdoor, or membrane channel, that specializes in granting entry to a membrane componentknown as glycerol. Specifically the channel is called the glycerol facilitator (GlpF), from thebacterium Escherichia coli.
Bearing three alcohol groups, glycerol is a basic building block for the cell membrane. (Othercomponents include fatty acids and small charged molecules.) And not just in E. coli. Indeed,although the channel the researchers studied is from a bacterium, it belongs to a largeprotein family dubbed the aquaporins, which are found in species ranging from bacteria tohumans.
GlpF is highly specific for glycerol and similar polyalcohols. Somehow, even though watermolecules are much smaller, they cannot enter. The new study reveals why. In order forglycerol to clear the four-channel configuration in the cell membrane, it must pass througha narrow selectivity filter in the center of a channel. Here it is surrounded by amino acids thatclosely match its own structure, which is hydrophilic ("water-loving") on one side andhydrophobic ("water-fearing") on the other. Water molecules, in contrast, can only passthrough this area in single file, which is not energetically favorable, because they like to bondto one another. And ions, which are charged, are unable to pass the "water-fearing" side of thechannel. This cell entrance, it seems, is truly exclusive.
The main purpose of the passage is to _________
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