ArticleThe Journal of biological chemistry2024
The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.
Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- DIA-Based Quantitative Proteomics Reveals Adaptive Responses and Potential Mechanisms of Se(IV) Resistance inMicroorganisms · 2026Article
- The structure of the SufBCbioRxiv : the preprint server for biology · 2026Article
- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- Adaptation of Fe-S Cluster Assembly to Rising OResearch square · 2026Article
- Characterization of a mechanistic connection between persulfide transfer and ATP hydrolysis in the SufBC2D scaffold of the Suf Fe-S cluster assembly pathway.Metallomics : integrated biometal science · 2025Article
- Mycobacterium tuberculosis sulfurtransferase SseA is activated by its neighboring gene product Rv3284.FEBS letters · 2025Article
- A Role for Two Conserved Arginine Residues in Protected Persulfide Transfer by SufE-Dependent SufS Cysteine Desulfurases.Biochemistry · 2025Article
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Abstract
Fe-S clusters are critical cofactors for redox chemistry in all organisms. The cysteine desulfurase, SufS, provides sulfur in the SUF Fe-S cluster bioassembly pathway. SufS is a dimeric, pyridoxal 5'-phosphate-dependent enzyme that uses cysteine as a substrate to generate alanine and a covalent persulfide on an active site cysteine residue. SufS enzymes are activated by an accessory transpersulfurase protein, either SufE or SufU depending on the organism, which accepts the persulfide product and delivers it to downstream partners for Fe-S assembly. Here, using Escherichia coli proteins, we present the first X-ray crystal structure of a SufS/SufE complex. There is a 1:1 stoichiometry with each monomeric unit of the EcSufS dimer bound to one EcSufE subunit, though one EcSufE is rotated ∼7° closer to the EcSufS active site. EcSufE makes clear interactions with the α16 helix of EcSufS and site-directed mutants of several α16 residues were deficient in EcSufE binding. Analysis of the EcSufE structure showed a loss of electron density at the EcSufS/EcSufE interface for a flexible loop containing the highly conserved residue R119. An R119A EcSufE variant binds EcSufS but is not active in cysteine desulfurase assays and fails to support Fe-S cluster bioassembly in vivo.
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