The Alternating Access Transport Mechanism in LacY

The Alternating Access Transport Mechanism in LacY,10.1007/s00232-010-9327-5,Journal of Membrane Biology,H. Ronald Kaback,Irina Smirnova,Vladimir Kash

The Alternating Access Transport Mechanism in LacY   (Citations: 1)
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Lactose permease of Escherichia coli (LacY) is highly dynamic, and sugar binding causes closing of a large inward-facing cavity with opening of a wide outward-facing hydrophilic cavity. Therefore, lactose/H+ symport via LacY very likely involves a global conformational change that allows alternating access of single sugar- and H+-binding sites to either side of the membrane. Here, in honor of Stephan H. White’s seventieth birthday, we review in camera the various biochemical/biophysical approaches that provide experimental evidence for the alternating access mechanism.
Journal: Journal of Membrane Biology - J MEMBRANE BIOL , vol. 239, no. 1, pp. 85-93, 2011
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