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- W3004582793 abstract "The makeup of the gram-negative cell envelope, with an outer-leaflet composed of bulky lipopolysaccharides (LPS), has strong connotations for the outer membrane proteins (OMPs) within it. In our recent work on the E. coli cobalamin transporter BtuB, we have demonstrated the ability to attach one or more methanethiosulfonate (MTSL) spin-labels to the protein in vivo for use in electron paramagnetic resonance (EPR). Specifically, this enables the extraction of both intra- and inter-molecular distance information using the pulsed-EPR Double Electron-Electron Resonance (DEER) technique. BtuB is a slightly oblong beta-barrel, and by attaching single spin-labels around its circumference we have found evidence for long-distance interactions consistent with inter-molecular organization of the protein on the cell surface. Additionally, the distance distributions are altered when the protein is expressed using a strain with altered disulfide-bond formation and cell division kinetics, indicating that the organizational mode is dependent on the state of the cell envelope. Like other TonB dependent transporters (TBDTs), the BtuB barrel surrounds a central, globular hatch domain through which the substrates must pass via an unknown mechanism. To probe this, we also determined intra-molecular distances both across the barrel and between the hatch and the barrel in response to substrate. While we have found evidence for a substrate-dependent helical shift in an upper hatch loop, most of the extracellular hatch and barrel sites are conformationally restricted in the cellular environment. Intriguingly, the periplasmic face of the protein instead displays additional flexibility in the cell. These initially contradictory results appear to be linked to the native environment and may result from interactions with neighboring LPS molecules." @default.
- W3004582793 created "2020-02-14" @default.
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- W3004582793 date "2020-02-01" @default.
- W3004582793 modified "2023-09-27" @default.
- W3004582793 title "EPR Distance Measurements on the E. coli Cobalamin Transporter BtuB Indicate Conformation and Organization are Dependent on the Native, Cellular Environment" @default.
- W3004582793 doi "https://doi.org/10.1016/j.bpj.2019.11.1253" @default.
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