Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF
Bacteria deploy weapons to kill their neighbours during competition for resources and to aid survival within microbiomes. Colicins were the first such antibacterial system identified, yet how these bacteriocins cross the outer membrane (OM) of Escherichia coli is unknown. Here, by solving the struct...
Κύριοι συγγραφείς: | Francis, M-LR, Webby, MN, Housden, NG, Kaminska, R, Elliston, E, Chinthammit, B, Lukoyanova, N, Kleanthous, C |
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Μορφή: | Journal article |
Γλώσσα: | English |
Έκδοση: |
EMBO Press
2021
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Παρόμοια τεκμήρια
Παρόμοια τεκμήρια
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Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.
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Orientation of the OmpF porin in planar lipid bilayers
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Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF.
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Έκδοση: (2010) -
OmpF enhances the ability of BtuB to protect susceptible Escherichia coli cells from colicin E9 cytotoxicity.
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