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Author Correction: The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes

The Original Article was published on 29 June 2020

Correction to: Nature Chemical Biology https://doi.org/10.1038/s41589-020-0569-y, published online 29 June 2020

In the version of this article originally published, some information regarding Fig. 5 was switched around. The figure citation in the sentence “Based on the biochemical and structural data, we propose the following mechanism for epimerization in bottromycin biosynthesis (Fig. 5b)” should refer to Fig. 5a instead of 5b. Additionally, the text for panels a and b in the legend for Fig. 5 were swapped. The legend should read “a, Proposed mechanism for the epimerization of 3b to yield 3a. BotH residues are labeled in black and substrate residues in blue. Hydrogen bonds are shown as dashed lines. Ordered water molecules surrounding the Asp7 carboxy group are not shown for clarity (see Extended Data Fig. 5 for details). b, Proposed role of BotH in self-resistance. A rise of intracellular bottromycin concentrations leads to inhibition of BotH epimerase activity, which may in turn prevent self-poisoning of the producing strain. BotH may also act as an intracellular buffer to store bottromycins.” The errors have been corrected.

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Correspondence to Jesko Koehnke.

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Sikandar, A., Franz, L., Adam, S. et al. Author Correction: The bottromycin epimerase BotH defines a group of atypical α/β-hydrolase-fold enzymes. Nat Chem Biol 16, 1034 (2020). https://doi.org/10.1038/s41589-020-0624-8

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