Function
Cysteine desulfurase (Suf) catalyzes the conversion of L-cysteine to L-alanine and sulfane sulfur. Suf is part of the iron-sulfur cluster complex where SufS transfers the sulphide from Cys to SufU which is a scaffold protein[1]. In E. coli, SufE stimulates the activity of SufS[2]. Suf has a role in the biosynthesis of Fe-S custers, thiamine, thionucleosides, biotin, lipoic acid, molybdopterin and NAD[3]. Suf is a PLP-dependent enzyme.
Structural highlights
The structure of SufS contains the cofactor PLP bound to Lys224.
Cys361 is the nucleophilic catalytic residue. The reaction product alanine is bound near the Cys361-persulfide[4].
3D structures of cysteine desulfurase
Cysteine desulfurase 3D structures
- ↑ Albrecht AG, Peuckert F, Landmann H, Miethke M, Seubert A, Marahiel MA. Mechanistic characterization of sulfur transfer from cysteine desulfurase SufS to the iron-sulfur scaffold SufU in Bacillus subtilis. FEBS Lett. 2011 Feb 4;585(3):465-70. doi: 10.1016/j.febslet.2011.01.005. Epub, 2011 Jan 12. PMID:21236255 doi:https://dx.doi.org/10.1016/j.febslet.2011.01.005
- ↑ Outten FW, Wood MJ, Munoz FM, Storz G. The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli. J Biol Chem. 2003 Nov 14;278(46):45713-9. Epub 2003 Aug 26. PMID:12941942 doi:https://dx.doi.org/10.1074/jbc.M308004200
- ↑ Mihara H, Esaki N. Bacterial cysteine desulfurases: their function and mechanisms. Appl Microbiol Biotechnol. 2002 Oct;60(1-2):12-23. doi:, 10.1007/s00253-002-1107-4. Epub 2002 Sep 4. PMID:12382038 doi:https://dx.doi.org/10.1007/s00253-002-1107-4
- ↑ Blauenburg B, Mielcarek A, Altegoer F, Fage CD, Linne U, Bange G, Marahiel MA. Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU. PLoS One. 2016 Jul 6;11(7):e0158749. doi: 10.1371/journal.pone.0158749., eCollection 2016. PMID:27382962 doi:https://dx.doi.org/10.1371/journal.pone.0158749
