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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...

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Hlavní autoři: Weinglass, Adam B., Kaback, H. Ronald
Médium: Artigo
Jazyk:Inglês
Vydáno: The National Academy of Sciences 1999
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC18007/
https://ncbi.nlm.nih.gov/pubmed/10500150
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