4Q75
Crystal structure of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana
Summary for 4Q75
Entry DOI | 10.2210/pdb4q75/pdb |
Related | 4Q76 |
Descriptor | Cysteine desulfurase 2, chloroplastic (2 entities in total) |
Functional Keywords | cysteine desulfurase, atsufe1, chloroplast, transferase |
Biological source | Arabidopsis thaliana (mouse-ear cress,thale-cress) |
Cellular location | Plastid, chloroplast: Q93WX6 |
Total number of polymer chains | 2 |
Total formula weight | 94418.59 |
Authors | Roret, T.,Didierjean, C. (deposition date: 2014-04-24, release date: 2014-09-10, Last modification date: 2023-12-06) |
Primary citation | Roret, T.,Pegeot, H.,Couturier, J.,Mulliert, G.,Rouhier, N.,Didierjean, C. X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana. Acta Crystallogr F Struct Biol Commun, 70:1180-1185, 2014 Cited by PubMed 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. PubMed: 25195888DOI: 10.1107/S2053230X14017026 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.709 Å) |
Structure validation
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