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TonB induces conformational changes in surface-exposed loops of FhuA, outer membrane receptor of Escherichia coli
FhuA, outer membrane receptor of Escherichia coli, transports hydroxamate-type siderophores into the periplasm. Cytoplasmic membrane–anchored TonB transduces energy to FhuA to facilitate siderophore transport. Because the N-terminal cork domain of FhuA occludes the C-terminal β-barrel lumen, conform...
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| Hlavní autoři: | , , , , |
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| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Cold Spring Harbor Laboratory Press
2008
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2548371/ https://ncbi.nlm.nih.gov/pubmed/18653801 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1110/ps.036244.108 |
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