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4Q75

Crystal structure of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana

Summary for 4Q75
Entry DOI10.2210/pdb4q75/pdb
Related4Q76
DescriptorCysteine desulfurase 2, chloroplastic (2 entities in total)
Functional Keywordscysteine desulfurase, atsufe1, chloroplast, transferase
Biological sourceArabidopsis thaliana (mouse-ear cress,thale-cress)
Cellular locationPlastid, chloroplast: Q93WX6
Total number of polymer chains2
Total formula weight94418.59
Authors
Roret, T.,Didierjean, C. (deposition date: 2014-04-24, release date: 2014-09-10, Last modification date: 2023-12-06)
Primary citationRoret, 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: 25195888
DOI: 10.1107/S2053230X14017026
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.709 Å)
Structure validation

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数据于2025-07-09公开中

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