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The plug domain of FepA, a TonB-dependent transport protein from Escherichia coli, binds its siderophore in the absence of the transmembrane barrel domain

FepA, an outer membrane iron siderophore transporter from Escherichia coli, is composed of a 22-stranded membrane-spanning β barrel with a globular N-terminal “plug” domain of 148 residues that folds up inside the barrel and completely occludes the barrel's interior (1). We have overexpressed and pu...

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書誌詳細
出版年:Proc Natl Acad Sci U S A
主要な著者: Usher, Ken C., Özkan, Engin, Gardner, Kevin H., Deisenhofer, Johann
フォーマット: Artigo
言語:Inglês
出版事項: National Academy of Sciences 2001
主題:
オンライン・アクセス:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC58525/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11526207/
https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.181353398
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