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X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana

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 beta-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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Thomas Roret, Henri Pégeot, Jérémy Couturier, Guillermo Mulliert, Nicolas Rouhier, et al.. X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, International Union of Crystallography, 2014, 70 (9), pp.1180-1185. ⟨10.1107/S2053230X14017026⟩. ⟨hal-01521313⟩



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