Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2189747 | Journal of Molecular Biology | 2006 | 9 Pages |
Abstract
Building a three-dimensional model of the sucrose permease of Escherichia coli (CscB) with the X-ray crystal structure lactose permease (LacY) as template reveals a similar overall fold for CscB. Moreover, despite only 28% sequence identity and a marked difference in substrate specificity, the structural organization of the residues involved in sugar-binding and H+ translocation is conserved in CscB. Functional analyses of mutants in the homologous key residues provide strong evidence that they play a similar critical role in the mechanisms of CscB and LacY.
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Authors
Viveka Vadyvaloo, Irina N. Smirnova, Vladimir N. Kasho, H. Ronald Kaback,