| Structural highlights
Function
SUFU_BACSU Its function is controversial. Has been generally assumed to be an iron-sulfur cluster assembly scaffold protein (PubMed:20097860, PubMed:21236255), but more recent evidence suggest it is a sulfurtransferase rather than a scaffold assembly protein (PubMed:24321018). Has been shown to bind low levels of a labile, air-sensitive Fe-S cluster; this can be assembled under anaerobic conditions from FeCl(3) and Li(2)S. Has been shown to be able to transfer this Fe-S cluster to an acceptor protein. Stimulates the cysteine desulfurase activity of SufS, for which it acts as a second substrate. Alkylation eliminates its ability to stimulate SufS. A mixture of SufS, SufU, Fra and L-cysteine is able to reconstitute Fe-S clusters on apo-aconitase (citB), reconstituting aconitase activity.[1] [2] [3] [4] [5]
Publication Abstract from PubMed
SufU is a zinc-containing protein involved in mobilization of sulfur from SufS for iron-sulfur cluster biogenesis of Bacillus subtilis. Structural basis for the sulfur transfer in SufS-SufU complex was revealed. A zinc-ligand exchange reaction upon SufS-SufU complexation provides a free thiol from Cys41 of SufU as a sulfur acceptor.
Zinc-Ligand Swapping Mediated Complex Formation and Sulfur Transfer between SufS and SufU for Iron-Sulfur Cluster Biogenesis in Bacillus subtilis.,Fujishiro T, Terahata T, Kunichika K, Yokoyama N, Maruyama C, Asai K, Takahashi Y J Am Chem Soc. 2017 Dec 13. doi: 10.1021/jacs.7b11307. PMID:29235855[6]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Albrecht AG, Netz DJ, Miethke M, Pierik AJ, Burghaus O, Peuckert F, Lill R, Marahiel MA. SufU is an essential iron-sulfur cluster scaffold protein in Bacillus subtilis. J Bacteriol. 2010 Mar;192(6):1643-51. doi: 10.1128/JB.01536-09. Epub 2010 Jan 22. PMID:20097860 doi:http://dx.doi.org/10.1128/JB.01536-09
- ↑ Selbach B, Earles E, Dos Santos PC. Kinetic analysis of the bisubstrate cysteine desulfurase SufS from Bacillus subtilis. Biochemistry. 2010 Oct 12;49(40):8794-802. doi: 10.1021/bi101358k. Epub 2010 Sep , 16. PMID:20822158 doi:http://dx.doi.org/10.1021/bi101358k
- ↑ 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:http://dx.doi.org/10.1016/j.febslet.2011.01.005
- ↑ Albrecht AG, Landmann H, Nette D, Burghaus O, Peuckert F, Seubert A, Miethke M, Marahiel MA. The frataxin homologue Fra plays a key role in intracellular iron channeling in Bacillus subtilis. Chembiochem. 2011 Sep 5;12(13):2052-61. doi: 10.1002/cbic.201100190. Epub 2011, Jul 8. PMID:21744456 doi:http://dx.doi.org/10.1002/cbic.201100190
- ↑ Selbach BP, Chung AH, Scott AD, George SJ, Cramer SP, Dos Santos PC. Fe-S cluster biogenesis in Gram-positive bacteria: SufU is a zinc-dependent sulfur transfer protein. Biochemistry. 2014 Jan 14;53(1):152-60. doi: 10.1021/bi4011978. Epub 2013 Dec 23. PMID:24321018 doi:http://dx.doi.org/10.1021/bi4011978
- ↑ Fujishiro T, Terahata T, Kunichika K, Yokoyama N, Maruyama C, Asai K, Takahashi Y. Zinc-Ligand Swapping Mediated Complex Formation and Sulfur Transfer between SufS and SufU for Iron-Sulfur Cluster Biogenesis in Bacillus subtilis. J Am Chem Soc. 2017 Dec 13. doi: 10.1021/jacs.7b11307. PMID:29235855 doi:http://dx.doi.org/10.1021/jacs.7b11307
|
