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• W2016090532 abstract "The FeoB family of membrane embedded G proteins are involved with high affinity Fe(II) uptake in prokaryotes. Here, we report that FeoB harbors a novel GDP dissociation inhibitor-like domain that specifically stabilizes GDP-binding through an interaction with the switch I region of the G protein. We show that the stabilization of GDP binding is conserved between species despite a high degree of sequence variability in their guanine nucleotide dissociation inhibitor (GDI)-like domains, and demonstrate that the presence of the membrane embedded domain increases GDP-binding affinity roughly 150-fold over the level accomplished by action of the GDI-like domain alone. To our knowledge, this is the first example for a prokaryotic GDI, targeting a bacterial G protein-coupled membrane process. Our findings suggest that Fe(II) uptake in bacteria involves a G protein regulatory pathway reminiscent of signaling mechanisms found in higher-order organisms." @default.
• W2016090532 created "2016-06-24" @default.
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• W2016090532 date "2008-01-01" @default.
• W2016090532 modified "2023-09-29" @default.
• W2016090532 title "Characterization of a Novel Prokaryotic GDP Dissociation Inhibitor Domain from the G Protein Coupled Membrane Protein FeoB" @default.
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• W2016090532 doi "https://doi.org/10.1016/j.jmb.2007.11.027" @default.
• W2016090532 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2266681" @default.
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