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- W2074592237 abstract "G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes." @default.
- W2074592237 created "2016-06-24" @default.
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- W2074592237 date "2009-07-23" @default.
- W2074592237 modified "2023-10-03" @default.
- W2074592237 title "Structural basis of GDP release and gating in G protein coupled Fe2+ transport" @default.
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- W2074592237 doi "https://doi.org/10.1038/emboj.2009.208" @default.
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