Correction to: Nature Communications https://doi.org/10.1038/s41467-022-33988-1, published online 21 October 2022
The original version of this Article contained an error in the introduction, which incorrectly stated ‘Quantum mechanics/molecular mechanics (QM/MM) simulations of this enzyme do indicate participation of Glu303 in the mechanism, but the covalent-like interaction is highly transitory, lasting only for only a few picoseconds8 and mutation of this residue to cysteine or aspartate only slightly slows the reaction9.’ The correct version states ‘Quantum mechanics/molecular mechanics (QM/MM) metadynamics analysis of a bovine GT-6’s mechanism predicts that, while the substrates are organized very similarly to other retaining GTs, the donor saccharide forms an intermediate glutamate-galactose covalent adduct prior to transfer to the acceptor8; however, in later experiments on human GT-6, mutation of Glu303 to cysteine or aspartate was found to only slightly slow the reaction9.’
This has been corrected in both the PDF and HTML versions of the Article.
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Forrester, T.J.B., Ovchinnikova, O.G., Li, Z. et al. Author Correction: The retaining β-Kdo glycosyltransferase WbbB uses a double-displacement mechanism with an intermediate adduct rearrangement step. Nat Commun 13, 7686 (2022). https://doi.org/10.1038/s41467-022-35491-z
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DOI: https://doi.org/10.1038/s41467-022-35491-z
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