ArticleBiochemistry2019
Structural Evidence for Dimer-Interface-Driven Regulation of the Type II Cysteine Desulfurase, SufS.
Article in Biochemistry, 2019. 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, 14 citations in OpenAlex.
- Development of a Spectrophotometric Assay for the Cysteine Desulfurase fromAntibiotics (Basel, Switzerland) · 2025Article
- Two Cysteines in Raf Kinase Inhibitor Protein Make Differential Contributions to Structural Dynamics In Vitro.Molecules (Basel, Switzerland) · 2025Article
- The structural and functional analysis of mycobacteria cysteine desulfurase-loaded encapsulin.Communications biology · 2024Article
- Structural and Biochemical Characterization ofBiomolecules · 2023Article
- Roles of conserved active site residues in the IscS cysteine desulfurase reaction.Frontiers in microbiology · 2023Article
- Structural and Biochemical Characterization ofACS omega · 2022Article
- Structural diversity of cysteine desulfurases involved in iron-sulfur cluster biosynthesis.Biophysics and physicobiology · 2022Article
- The Multifaceted Bacterial Cysteine Desulfurases: From Metabolism to Pathogenesis.Antioxidants (Basel, Switzerland) · 2021Review
- Fe-S cluster biogenesis by the bacterial Suf pathway.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases.Acta crystallographica. Section D, Structural biology · 2020Article
- Direct observation of intermediates in the SufS cysteine desulfurase reaction reveals functional roles of conserved active-site residues.The Journal of biological chemistry · 2019Article
- Hydrogen Sulfide From Cysteine Desulfurase, Not 3-Mercaptopyruvate Sulfurtransferase, Contributes to Sustaining Cell Growth and Bioenergetics inFrontiers in microbiology · 2019Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
SufS is a type II cysteine desulfurase and acts as the initial step in the Suf Fe-S cluster assembly pathway. In Escherichia coli, this pathway is utilized under conditions of oxidative stress and is resistant to reactive oxygen species. Mechanistically, this means SufS must shift between protecting a covalent persulfide intermediate and making it available for transfer to the next protein partner in the pathway, SufE. Here, we report five X-ray crystal structures of SufS including a new structure of SufS containing an inward-facing persulfide intermediate on C364. Additional structures of SufS variants with substitutions at the dimer interface show changes in dimer geometry and suggest a conserved β-hairpin structure plays a role in mediating interactions with SufE. These new structures, along with previous HDX-MS and biochemical data, identify an interaction network capable of communication between active-sites of the SufS dimer coordinating the shift between desulfurase and transpersulfurase activities.
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