ArticleJournal of molecular biology2008
Characterization of a novel prokaryotic GDP dissociation inhibitor domain from the G protein coupled membrane protein FeoB.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 48 citations in OpenAlex.
- The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025Article
- Characterization of intact FeoB in a lipid bilayer using styrene-maleic acid (SMA) copolymers.Biochimica et biophysica acta. Biomembranes · 2025Article
- Structural Determinants ofbioRxiv : the preprint server for biology · 2024Article
- Functional Characterization of FeoAB in Iron Acquisition and Pathogenicity in Riemerella anatipestifer.Microbiology spectrum · 2023Article
- AI-driven pan-proteome analyses reveal insights into the biohydrometallurgical properties ofFrontiers in microbiology · 2023Article
- A general protocol for the expression and purification of the intact transmembrane transporter FeoB.Biochimica et biophysica acta. Biomembranes · 2022Article
- The structure of Vibrio cholerae FeoC reveals conservation of the helix-turn-helix motif but not the cluster-binding domain.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Vanadate inhibits Feo-mediated iron transport in Vibrio cholerae.Metallomics : integrated biometal science · 2021Article
- Bacterial iron detoxification at the molecular level.The Journal of biological chemistry · 2020Review
- Article
- Toward a mechanistic understanding of Feo-mediated ferrous iron uptake.Metallomics : integrated biometal science · 2018Review
- Vibrio cholerae FeoA, FeoB, and FeoC Interact To Form a Complex.Journal of bacteriology · 2016Article
- Structural model of FeoB, the iron transporter from Pseudomonas aeruginosa, predicts a cysteine lined, GTP-gated pore.Bioscience reports · 2016Article
- An update on the transport and metabolism of iron in Listeria monocytogenes: the role of proteins involved in pathogenicity.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2015Review
- FeoA and FeoC are essential components of the Vibrio cholerae ferrous iron uptake system, and FeoC interacts with FeoB.Journal of bacteriology · 2013Article
- Perceived social support among people with physical disability.Iranian Red Crescent medical journal · 2013Article
- Structure of an atypical FeoB G-domain reveals a putative domain-swapped dimer.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Solution structure of Escherichia coli FeoA and its potential role in bacterial ferrous iron transport.Journal of bacteriology · 2013Article
- Crystal structure of the Klebsiella pneumoniae NFeoB/FeoC complex and roles of FeoC in regulation of Fe2+ transport by the bacterial Feo system.Journal of bacteriology · 2012Article
- The structure of an N11A mutant of the G-protein domain of FeoB.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.