ArticleActa crystallographica. Section F, Structural biology communications2014
X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana.
Article in Acta crystallographica. Section F, Structural biology communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 15 citations in OpenAlex.
- HAntioxidants & redox signaling · 2023Article
- Structural evidence for a latch mechanism regulating access to the active site of SufS-family cysteine desulfurases.Acta crystallographica. Section D, Structural biology · 2020Article
- Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Snapshots of C-S Cleavage in Egt2 Reveals Substrate Specificity and Reaction Mechanism.Cell chemical biology · 2018Article
- Assembly and Transfer of Iron-Sulfur Clusters in the Plastid.Frontiers in plant science · 2018Review
- Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.Nature communications · 2017Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The chloroplastic Arabidopsis thaliana Nfs2 (AtNfs2) is a group II pyridoxal 5'-phosphate-dependent cysteine desulfurase that is involved in the initial steps of iron-sulfur cluster biogenesis. The group II cysteine desulfurases require the presence of sulfurtransferases such as SufE proteins for optimal activity. Compared with group I cysteine desulfurases, proteins of this group contains a smaller extended lobe harbouring the catalytic cysteine and have a β-hairpin constraining the active site. Here, two crystal structures of AtNfs2 are reported: a wild-type form with the catalytic cysteine in a persulfide-intermediate state and a C384S variant mimicking the resting state of the enzyme. In both structures the well conserved Lys241 covalently binds pyridoxal 5'-phosphate, forming an internal aldimine. Based on available homologous bacterial complexes, a model of a complex between AtNfs2 and the SufE domain of its biological partner AtSufE1 is proposed, revealing the nature of the binding sites.
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