ArticlePloS one2011
Ferritin structure from Mycobacterium tuberculosis: comparative study with homologues identifies extended C-terminus involved in ferroxidase activity.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 61 citations in OpenAlex.
- Unveiling Structural Heterogeneity and Evolutionary Adaptations of Heteromultimeric Bacterioferritin Nanocages.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Iron mobilization from intact ferritin: effect of differential redox activity of quinone derivatives with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Bacterioferritin nanocage structures uncover the biomineralization process in ferritins.PNAS nexus · 2023Article
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- Identification of FtpA, a Dps-Like Protein Involved in Anti-Oxidative Stress and Virulence in Actinobacillus pleuropneumoniae.Journal of bacteriology · 2022Article
- The Iron Response ofFrontiers in cellular and infection microbiology · 2022Review
- Mycobacterium tuberculosis ferritin: a suitable workhorse protein for cryo-EM development.Acta crystallographica. Section D, Structural biology · 2021Article
- Flavin-mediated reductive iron mobilization from frog M and Mycobacterial ferritins: impact of their size, charge and reactivities with NADH/OJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2021Article
- Structural comparison of two ferritins from the marine invertebrate Phascolosoma esculenta.FEBS open bio · 2021Article
- Shotgun EM of mycobacterial protein complexes during stationary phase stress.Current research in structural biology · 2020Article
- Heme and hemoglobin utilization by Mycobacterium tuberculosis.Nature communications · 2019Article
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- Protein 3D Structure and Electron Microscopy Map Retrieval Using 3D-SURFER2.0 and EM-SURFER.Current protocols in bioinformatics · 2017Article
- Systematic Identification ofMolecular & cellular proteomics : MCP · 2017Article
- Biological iron-sulfur storage in a thioferrate-protein nanoparticle.Nature communications · 2017Article
- Differential Roles of Iron Storage Proteins in Maintaining the Iron Homeostasis in Mycobacterium tuberculosis.PloS one · 2017Article
- The mycobacterial iron-dependent regulator IdeR induces ferritin (bfrB) by alleviating Lsr2 repression.Molecular microbiology · 2015Article
- Fe(2+) substrate transport through ferritin protein cage ion channels influences enzyme activity and biomineralization.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- The B-type channel is a major route for iron entry into the ferroxidase center and central cavity of bacterioferritin.The Journal of biological chemistry · 2015Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Ferritins are recognized as key players in the iron storage and detoxification processes. Iron acquisition in the case of pathogenic bacteria has long been established as an important virulence mechanism. Here, we report a 3.0 Å crystal structure of a ferritin, annotated as Bacterioferritin B (BfrB), from Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis that continues to be one of the world's deadliest diseases. Similar to the other members of ferritin family, the Mtb BfrB subunit exhibits the characteristic fold of a four-helical bundle that possesses the ferroxidase catalytic centre. We compare the structure of Mtb BfrB with representatives of the ferritin family belonging to the archaea, eubacteria and eukarya. Unlike most other ferritins, Mtb BfrB has an extended C-terminus. To dissect the role of this extended C-terminus, truncated Mtb BfrB was purified and biochemical studies implicate this region in ferroxidase activity and iron release in addition to providing stability to the protein. Functionally important regions in a protein of known 3D-structure can be determined by estimating the degree of conservation of the amino-acid sites with its close homologues. Based on the comparative studies, we identify the slowly evolving conserved sites as well as the rapidly evolving variable sites and analyze their role in relation to structure and function of Mtb BfrB. Further, electrostatic computations demonstrate that although the electrostatic environment of catalytic residues is preserved within the family, extensive variability is exhibited by residues defining the channels and pores, in all likelihood keeping up with the diverse functions executed by these ferritins in varied environments.
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