3fhk
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Crystal structure of APC1446, B.subtilis YphP disulfide isomerase
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Structural highlights
FunctionBRXA_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
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This page was last modified 09:49, 21 February 2024.