Structural highlights
Function
BRXA_BACSU S-bacillithiolation is the formation of mixed disulfide bonds between protein thiols and the general thiol reductant bacillithiol (BSH) under oxidative stress. BSH is an equivalent of glutathione (GSH) in Firmicutes. This protein is a dithiol bacilliredoxin, which debacillithiolates (removes BSH) the S-bacillithiolated OhrR (OhrR-SSB) in vitro and in vivo NaOCl-generated S-bacillithiolated MetE (MetE-SSB). Involved in maintaining redox homeostasis in response to disulfide stress conditions (PubMed:24313874). Has a redox potential of -130 mV. Displays weak protein disulfide isomerase activity in vitro (PubMed:19653655).[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Derewenda U, Boczek T, Gorres KL, Yu M, Hung LW, Cooper D, Joachimiak A, Raines RT, Derewenda ZS. Structure and Function of Bacillus subtilis YphP, a Prokaryotic Disulfide Isomerase with a CXC Catalytic Motif (,). Biochemistry. 2009 Aug 21. PMID:19653655 doi:10.1021/bi900437z
- ↑ Gaballa A, Chi BK, Roberts AA, Becher D, Hamilton CJ, Antelmann H, Helmann JD. Redox regulation in Bacillus subtilis: The bacilliredoxins BrxA(YphP) and BrxB(YqiW) function in de-bacillithiolation of S-bacillithiolated OhrR and MetE. Antioxid Redox Signal. 2014 Jul 20;21(3):357-67. PMID:24313874 doi:10.1089/ars.2013.5327
