Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.
Porins are β-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin O...
主要な著者: | Housden, N, Hopper, J, Lukoyanova, N, Rodriguez-Larrea, D, Wojdyla, J, Klein, A, Kaminska, R, Bayley, H, Saibil, H, Robinson, C, Kleanthous, K |
---|---|
フォーマット: | Journal article |
言語: | English |
出版事項: |
2013
|
類似資料
-
Orientation of the OmpF porin in planar lipid bilayers
著者:: Ionescu, S, 等
出版事項: (2017) -
Directed epitope delivery across the Escherichia coli outer membrane through the porin OmpF.
著者:: Housden, N, 等
出版事項: (2010) -
Porin threading drives receptor disengagement and establishes active colicin transport through Escherichia coli OmpF
著者:: Francis, M-LR, 等
出版事項: (2021) -
Lipid binding attenuates channel closure of the outer membrane protein OmpF
著者:: Liko, I, 等
出版事項: (2018) -
Bifurcated binding of the OmpF receptor underpins import of the bacteriocin colicin N into Escherichia coli
著者:: Jansen, KB, 等
出版事項: (2020)