ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structure of an atypical FeoB G-domain reveals a putative domain-swapped dimer.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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
7 citing papers in PubMed.
- 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
- A general protocol for the expression and purification of the intact transmembrane transporter FeoB.Biochimica et biophysica acta. Biomembranes · 2022Article
- Studies on the X-Ray and Solution Structure of FeoB from Escherichia coli BL21.Biophysical journal · 2016Article
- 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
- Transport proteins promoting Escherichia coli pathogenesis.Microbial pathogenesisArticle
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Authors and funding
6 authors.
Funding
Abstract
FeoB is a transmembrane protein involved in ferrous iron uptake in prokaryotic organisms. FeoB comprises a cytoplasmic soluble domain termed NFeoB and a C-terminal polytopic transmembrane domain. Recent structures of NFeoB have revealed two structural subdomains: a canonical GTPase domain and a five-helix helical domain. The GTPase domain hydrolyses GTP to GDP through a well characterized mechanism, a process which is required for Fe(2+) transport. In contrast, the precise role of the helical domain has not yet been fully determined. Here, the structure of the cytoplasmic domain of FeoB from Gallionella capsiferriformans is reported. Unlike recent structures of NFeoB, the G. capsiferriformans NFeoB structure is highly unusual in that it does not contain a helical domain. The crystal structures of both apo and GDP-bound protein forms a domain-swapped dimer.
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