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...
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| Publicado no: | Proc Natl Acad Sci U S A |
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| Principais autores: | , |
| Formato: | Artigo |
| Idioma: | Inglês |
| Publicado em: |
National Academy of Sciences
1999
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| Assuntos: | |
| Acesso em linha: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC18007/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/10500150/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.96.20.11178 |
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