PMID:14630326
| Citation |
Abramson, J, Smirnova, I, Kasho, V, Verner, G, Iwata, S and Kaback, HR (2003) The lactose permease of Escherichia coli: overall structure, the sugar-binding site and the alternating access model for transport. FEBS Lett. 555:96-101 |
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| Abstract |
Membrane transport proteins transduce free energy stored in electrochemical ion gradients into a concentration gradient and are a major class of membrane proteins, many of which play important roles in human health and disease. Recently, the X-ray structure of the Escherichia coli lactose permease (LacY), an intensively studied member of a large group of related membrane transport proteins, was solved at 3.5 A. LacY is composed of N- and C-terminal domains, each with six transmembrane helices, symmetrically positioned within the molecule. The structure represents the inward-facing conformation, as evidenced by a large internal hydrophilic cavity open to the cytoplasmic side. The structure with a bound lactose homolog reveals the sugar-binding site in the cavity, and a mechanism for translocation across the membrane is proposed in which the sugar-binding site has alternating accessibility to either side of the membrane. |
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| Keywords |
Binding Sites; Biological Transport, Active; Carbohydrate Metabolism; Escherichia coli/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Membrane Transport Proteins/chemistry; Membrane Transport Proteins/metabolism; Models, Molecular; Monosaccharide Transport Proteins; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Static Electricity; Symporters; Thermodynamics |
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