Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF.
The porins OmpF and OmpC are trimeric β-barrel proteins with narrow channels running through each monomer that exclude molecules > 600 Da while mediating the passive diffusion of small nutrients and metabolites across the Gram-negative outer membrane (OM). Here, we elucidate the mechanism by...
Asıl Yazarlar: | Housden, N, Wojdyla, J, Korczynska, J, Grishkovskaya, I, Kirkpatrick, N, Brzozowski, A, Kleanthous, K |
---|---|
Materyal Türü: | Journal article |
Dil: | English |
Baskı/Yayın Bilgisi: |
2010
|
Benzer Materyaller
-
Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.
Yazar:: Housden, N, ve diğerleri
Baskı/Yayın Bilgisi: (2013) -
Orientation of the OmpF porin in planar lipid bilayers
Yazar:: Ionescu, S, ve diğerleri
Baskı/Yayın Bilgisi: (2017) -
Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF
Yazar:: Francis, M-LR, ve diğerleri
Baskı/Yayın Bilgisi: (2021) -
Bifurcated binding of the OmpF receptor underpins import of the bacteriocin colicin N into Escherichia coli
Yazar:: Jansen, KB, ve diğerleri
Baskı/Yayın Bilgisi: (2020) -
Lipid binding attenuates channel closure of the outer membrane protein OmpF
Yazar:: Liko, I, ve diğerleri
Baskı/Yayın Bilgisi: (2018)