ArticleJournal of structural biology2010
Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB.
Article in Journal of structural biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025Article
- The Coordination Chemistry of Two Peptidic Models of NFeoB and Core CFeoB Regions of FeoB Protein: Complexes of Fe(II), Mn(II), and Zn(II).Inorganic chemistry · 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
- Structures and coordination chemistry of transporters involved in manganese and iron homeostasis.Biochemical Society transactions · 2023Review
- Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.Biochemistry · 2021Review
- Genetic and structural determinants on iron assimilation pathways in the plant pathogen Xanthomonas citri subsp. citri and Xanthomonas sp.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2020Review
- The crystal structure of Klebsiella pneumoniae FeoA reveals a site for protein-protein interactions.Proteins · 2019Article
- Developing Colorimetric and Luminescence-Based High-Throughput Screening Platforms for Monitoring the GTPase Activity of Ferrous Iron Transport Protein B (FeoB).SLAS discovery : advancing life sciences R & D · 2019Article
- 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
- FeoA and FeoC are essential components of the Vibrio cholerae ferrous iron uptake system, and FeoC interacts with FeoB.Journal of bacteriology · 2013Article
- FeoC from Klebsiella pneumoniae contains a [4Fe-4S] cluster.Journal of bacteriology · 2013Article
- Structure of an atypical FeoB G-domain reveals a putative domain-swapped dimer.Acta crystallographica. Section F, Structural biology and crystallization communications · 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
- NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae.Journal of biomolecular NMR · 2012Article
- The structure of an N11A mutant of the G-protein domain of FeoB.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- The initiation of GTP hydrolysis by the G-domain of FeoB: insights from a transition-state complex structure.PloS one · 2011Article
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11 authors.
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Abstract
FeoB is a G-protein coupled membrane protein essential for Fe(II) uptake in prokaryotes. Here, we report the crystal structures of the intracellular domain of FeoB (NFeoB) from Klebsiella pneumoniae (KpNFeoB) and Pyrococcus furiosus (PfNFeoB) with and without bound ligands. In the structures, a canonical G-protein domain (G domain) is followed by a helical bundle domain (S-domain), which despite its lack of sequence similarity between species is structurally conserved. In the nucleotide-free state, the G-domain's two switch regions point away from the binding site. This gives rise to an open binding pocket whose shallowness is likely to be responsible for the low nucleotide-binding affinity. Nucleotide binding induced significant conformational changes in the G5 motif which in the case of GMPPNP binding was accompanied by destabilization of the switch I region. In addition to the structural data, we demonstrate that Fe(II)-induced foot printing cleaves the protein close to a putative Fe(II)-binding site at the tip of switch I, and we identify functionally important regions within the S-domain. Moreover, we show that NFeoB exists as a monomer in solution, and that its two constituent domains can undergo large conformational changes. The data show that the S-domain plays important roles in FeoB function.
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