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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY.

Cation-coupled active transport is an essential cellular process found ubiquitously in all living organisms. Here, we present two novel ligand-free X-ray structures of the lactose permease (LacY) of Escherichia coli determined at acidic and neutral pH, and propose a model for the mechanism of coupling between lactose and H+ translocation. No sugar-binding site is observed in the absence of ligand, and deprotonation of the key residue Glu269 is associated with ligand binding. Thus, substrate induces formation of the sugar-binding site, as well as the initial step in H+ transduction.[1]

References

  1. Structural evidence for induced fit and a mechanism for sugar/H+ symport in LacY. Mirza, O., Guan, L., Verner, G., Iwata, S., Kaback, H.R. EMBO J. (2006) [Pubmed]
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