Highlight | Chemistry | Structural biology
Conventionally, the detection of the intracellular hydrogen peroxide involves the oxidation of a sensor histidine. Exceptionally, PerR, the peroxide sensor encountered in Bacillus subtilis, detects the peroxide via the oxidation of a Fe2+ dependent histidine residue. Detailed analyzes of PerR have always been made complicated by the fact that two separate histidines are succeptibles to be oxidized. The purified protein is then composed of a mixure of non-oxidized, oxidized single and double oxidized forms. After optimizing the obtaining of the oxidized form of PerR at a single histidine, researchers at our institute obtained the first crystal structure of PerR harboring an oxo-histidine.
Traoré DA, El Ghazouani A, Jacquamet L, Borel F, Ferrer JL, Lascoux D, Ravanat JL, Jaquinod M, Blondin G, Caux-Thang C, Duarte V and Latour JM
Structural and functional characterization of 2-oxo-histidine in oxidized PerR protein.
Nature Chemical Biology, 2009
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