ArticleArchives of biochemistry and biophysics2020
Biochemical characterization of bacterial FeoBs: A perspective on nucleotide specificity.
Article in Archives of biochemistry and biophysics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- The structure of the full catalytic cycle ofbioRxiv : the preprint server for biology · 2025Article
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- Structural Determinants ofbioRxiv : the preprint server for biology · 2024Article
- Iron Homeostasis inBiology · 2023Review
- Functional Characterization of FeoAB in Iron Acquisition and Pathogenicity in Riemerella anatipestifer.Microbiology spectrum · 2023Article
- Divide and conquer: genetics, mechanism, and evolution of the ferrous iron transporter Feo inFrontiers in microbiology · 2023Article
- A general protocol for the expression and purification of the intact transmembrane transporter FeoB.Biochimica et biophysica acta. Biomembranes · 2022Article
- Identification of Key Functions Required for Production and Utilization of the Siderophore Piscibactin Encoded by the High-Pathogenicity IslandInternational journal of molecular sciences · 2022Article
- The role of nucleoside triphosphate hydrolase metallochaperones in making metalloenzymes.Metallomics : integrated biometal science · 2022Review
- Vanadate inhibits Feo-mediated iron transport in Vibrio cholerae.Metallomics : integrated biometal science · 2021Article
- Ins and Outs: Recent Advancements in Membrane Protein-Mediated Prokaryotic Ferrous Iron Transport.Biochemistry · 2021Review
- Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Iron is an essential requirement for the survival and virulence of most bacteria. The bacterial ferrous iron transporter protein FeoB functions as a major reduced iron transporter in prokaryotes, but its biochemical mechanism has not been fully elucidated. In the present study, we compared enzymatic properties of the cytosolic portions of pathogenic bacterial FeoBs to elucidate each bacterial strain-specific characteristic of the Feo system. We show that bacterial FeoBs are classified into two distinct groups that possess either a sole GTPase or an NTPase with a substrate promiscuity. This difference in nucleotide preference alters cellular requirements for monovalent and divalent cations. While the hydrolytic activity of the GTP-dependent FeoBs was stimulated by potassium, the action of the NTP-dependent FeoBs was not significantly affected by the presence of monovalent cations. Mutation of Asn11, having a role in potassium-dependent GTP hydrolysis, changed nucleotide specificity of the NTP-dependent FeoB, resulting in loss of ATPase activity. Sequence analysis suggested a possible association of alanine in the G5 motif for the NTP-dependent activity in FeoBs. This demonstration of the distinct enzymatic properties of bacterial FeoBs provides important insights into mechanistic details of Feo iron transport processes, as well as offers a promising species-specific anti-virulence target.
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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.