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Conformational flexibility at the substrate binding site in the lactose permease of Escherichia coli
Glu-126 (helix IV) and Arg-144 (helix V) are charge paired and play a critical role in substrate binding in the lactose permease of Escherichia coli. When Glu-126 is replaced with Asp, the permease has relatively high activity, implying that helix V has sufficient flexibility to allow Arg-144 to acc...
Sparad:
| Huvudupphovsmän: | , |
|---|---|
| Materialtyp: | Artigo |
| Språk: | Inglês |
| Publicerad: |
The National Academy of Sciences
1999
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| Ämnen: | |
| Länkar: | https://ncbi.nlm.nih.gov/pmc/articles/PMC18007/ https://ncbi.nlm.nih.gov/pubmed/10500150 |
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