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• W2052056124 endingPage "8721" @default.
• W2052056124 startingPage "8708" @default.
• W2052056124 abstract "To reduce peroxides, peroxiredoxins (Prxs) require a key “peroxidatic” Cys that, in a substrate-ready fully folded (FF) conformation, is oxidized to sulfenic acid and then, after a local unfolding (LU) of the active site, forms a disulfide bond with a second “resolving” Cys. For Salmonella typhimurium alkyl hydroperoxide reductase C (StAhpC) and some other Prxs, the FF structure is only known for a peroxidatic Cys→Ser variant, which may not accurately represent the wild-type enzyme. Here, we obtain the structure of authentic reduced wild-type StAhpC by dithiothreitol treatment of disulfide form crystals that fortuitously accommodate both the LU and FF conformations. The unique environment of one molecule in the crystal reveals a thermodynamic linkage between the folding of the active site loop and C-terminal regions, and comparisons with the Ser variant show structural and mobility differences from which we infer that the Cys→Ser mutation stabilizes the FF active site. A structure for the C165A variant (a resolving Cys to Ala mutant) in the same crystal form reveals that this mutation destabilizes the folding of the C-terminal region. These structures prove that subtle modifications to Prx structures can substantially influence enzymatic properties. We also present a simple thermodynamic framework for understanding the various mixtures of FF and LU conformations seen in these structures. On the basis of this framework, we rationalize how physiologically relevant regulatory post-translational modifications may modulate activity, and we propose a nonconventional strategy for designing selective Prx inhibitors." @default.
• W2052056124 created "2016-06-24" @default.
• W2052056124 creator A5022801498 @default.
• W2052056124 creator A5023232461 @default.
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• W2052056124 creator A5071279405 @default.
• W2052056124 creator A5074509343 @default.
• W2052056124 creator A5086284575 @default.
• W2052056124 date "2013-11-20" @default.
• W2052056124 modified "2023-09-26" @default.
• W2052056124 title "The Sensitive Balance between the Fully Folded and Locally Unfolded Conformations of a Model Peroxiredoxin" @default.
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• W2052056124 doi "https://doi.org/10.1021/bi4011573" @default.
• W2052056124 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3932808" @default.
• W2052056124 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24175952" @default.
• W2052056124 hasPublicationYear "2013" @default.
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• W2052056124 hasAuthorship W2052056124A5039556554 @default.
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