ArticleNature communications2024
Two-stage binding of mitochondrial ferredoxin-2 to the core iron-sulfur cluster assembly complex.
Article in Nature communications, 2024. 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.
- Higher-order structural organization of mitochondrial metabolism.The Journal of biological chemistry · 2026Review
- Nuclear translocation of mitochondrial ferredoxin reductase is regulated by AKT-mediated phosphorylation.The Biochemical journal · 2026Article
- Nanobodies as tools for studying human frataxin biology.Communications biology · 2026Article
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- NFS1 Plays a Critical Role in Regulating Ferroptosis Homeostasis.Biomolecules · 2025Review
- Structural insights into the Urm1-Uba4 pathway and its biological roles.Essays in biochemistry · 2025Review
- A novel mutation in FDX2 provides insights into the pathogenesis of MEOAL mitochondrial neuromuscular disease.Cell death & disease · 2025Article
- Iron-sulfur cluster biogenesis and regulation of intracellular iron homeostasis in Escherichia coli.Metallomics : integrated biometal science · 2025Review
- Comparative Structural Analysis of Escherichia Coli Cyay at Room and Cryogenic Temperatures Using Macromolecular and Serial Crystallography.Chembiochem : a European journal of chemical biology · 2025Article
- The cytochrome oxidase defect in ISC-depleted yeast is caused by impaired iron-sulfur cluster maturation of the mitoribosome assembly factor Rsm22.FEBS letters · 2025Article
- Two Key Ferredoxins for Nitrogen Fixation Have Different Specificities and Biophysical Properties.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Salutary Effects of Overexpression of Rsm22, an Assembly Factor for the Mitochondrial Ribosome, on Frataxin/Yfh1 Depletion Phenotypes inBiomolecules · 2025Article
- How to build a [2Fe-2S] cluster.Nature chemical biology · 2025Article
- OptimizedInternational journal of molecular sciences · 2025Article
- Frataxin: from the sequence to the biological role.Biophysical reviews · 2025Review
- A global perspective on research advances and future challenges in Friedreich ataxia.Nature reviews. Neurology · 2025Review
- Structural and Functional Perspectives on Mitochondrial LYR-Domain Proteins in Plants.Physiologia plantarumArticle
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Iron-sulfur (FeS) protein biogenesis in eukaryotes begins with the de novo assembly of [2Fe-2S] clusters by the mitochondrial core iron-sulfur cluster assembly (ISC) complex. This complex comprises the scaffold protein ISCU2, the cysteine desulfurase subcomplex NFS1-ISD11-ACP1, the allosteric activator frataxin (FXN) and the electron donor ferredoxin-2 (FDX2). The structural interaction of FDX2 with the complex remains unclear. Here, we present cryo-EM structures of the human FDX2-bound core ISC complex showing that FDX2 and FXN compete for overlapping binding sites. FDX2 binds in either a 'distal' conformation, where its helix F interacts electrostatically with an arginine patch of NFS1, or a 'proximal' conformation, where this interaction tightens and the FDX2-specific C terminus binds to NFS1, facilitating the movement of the [2Fe-2S] cluster of FDX2 closer to the ISCU2 FeS cluster assembly site for rapid electron transfer. Structure-based mutational studies verify the contact areas of FDX2 within the core ISC complex.
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