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...
保存先:
| 出版年: | Proc Natl Acad Sci U S A |
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| 主要な著者: | , , , |
| フォーマット: | Artigo |
| 言語: | Inglês |
| 出版事項: |
National Academy of Sciences
2001
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| 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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