ArticleThe Journal of biological chemistry2013
Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- The structure of the SufS-SufE complex reveals interactions driving protected persulfide transfer in iron-sulfur cluster biogenesis.bioRxiv : the preprint server for biology · 2024Article
- A widespread bacterial protein compartment sequesters and stores elemental sulfur.Science advances · 2024Article
- Structural and Biochemical Characterization ofBiomolecules · 2023Article
- Structural and Biochemical Characterization ofACS omega · 2022Article
- Possible molecular basis of the biochemical effects of cysteine-derived persulfides.Frontiers in molecular biosciences · 2022Review
- Structural diversity of cysteine desulfurases involved in iron-sulfur cluster biosynthesis.Biophysics and physicobiology · 2022Article
- Fe-S cluster biogenesis by the bacterial Suf pathway.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Structural Analysis of an l-Cysteine Desulfurase from an Ssp DNA Phosphorothioation System.mBio · 2020Article
- 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 and Persulfides Oxidation by Biologically Relevant Oxidizing Species.Antioxidants (Basel, Switzerland) · 2019Review
- Structural Evidence for Dimer-Interface-Driven Regulation of the Type II Cysteine Desulfurase, SufS.Biochemistry · 2019Article
- Changes in Protein Dynamics in Escherichia coli SufS Reveal a Possible Conserved Regulatory Mechanism in Type II Cysteine Desulfurase Systems.Biochemistry · 2018Article
- Iron-sulfur clusters biogenesis by the SUF machinery: close to the molecular mechanism understanding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Assembly and Transfer of Iron-Sulfur Clusters in the Plastid.Frontiers in plant science · 2018Review
- Insights into the inhibited form of the redox-sensitive SufE-like sulfur acceptor CsdE.PloS one · 2017Article
- Catalytic Intermediate Crystal Structures of Cysteine Desulfurase from the ArchaeonArchaea (Vancouver, B.C.) · 2017Article
- Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU.PloS one · 2016Article
- SufE D74R Substitution Alters Active Site Loop Dynamics To Further Enhance SufE Interaction with the SufS Cysteine Desulfurase.Biochemistry · 2015Article
- A novel cysteine desulfurase influencing organosulfur compounds in Lentinula edodes.Scientific reports · 2015Article
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In Escherichia coli, three cysteine desulfurases (IscS, SufS, and CsdA) initiate the delivery of sulfur for various biological processes such as the biogenesis of Fe-S clusters. The sulfur generated as persulfide on a cysteine residue of cysteine desulfurases is further transferred to Fe-S scaffolds (e.g. IscU) or to intermediate cysteine-containing sulfur acceptors (e.g. TusA, SufE, and CsdE) prior to its utilization. Here, we report the structures of CsdA and the CsdA-CsdE complex, which provide insight into the sulfur transfer mediated by the trans-persulfuration reaction. Analysis of the structures indicates that the conformational flexibility of the active cysteine loop in CsdE is essential for accepting the persulfide from the cysteine of CsdA. Additionally, CsdA and CsdE invoke a different binding mode than those of previously reported cysteine desulfurase (IscS) and sulfur acceptors (TusA and IscU). Moreover, the conservation of interaction-mediating residues between CsdA/SufS and CsdE/SufE further suggests that the SufS-SufE interface likely resembles that of CsdA and CsdE.
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