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Correction: Structural insights into a bacterial terpene cyclase fused with haloacid dehalogenase-like phosphatase
Keisuke Fujiyama
a,
Hiroshi Takagia,
Nhu Ngoc Quynh Voa,
Naoko Moritaa,
Toshihiko Nogawab and
Shunji Takahashi*a
aNatural Product Biosynthesis Research Unit, RIKEN Center for Sustainable Resource Science, Wako, Saitama, 351-0198, Japan. E-mail: shunjitaka@riken.jp
bMolecular Structure Characterization Unit, RIKEN Center for Sustainable Research Science, Wako, Saitama, 351-0198, Japan
First published on 26th November 2025
Abstract
Correction for ‘Structural insights into a bacterial terpene cyclase fused with haloacid dehalogenase-like phosphatase’ by Keisuke Fujiyama et al., Chem. Sci., 2025, 16, 15310–15319, https://doi.org/10.1039/d5sc04719f.
Upon publication of the original article, the authors were made aware that the preprint by Osika et al. (ref. 57 in our original manuscript) had been published,1 and is closely related to our study on drimenol synthase from Aquimarina spongiae (AsDMS). We hereby correct the sentence on page 15311, left column, line 20, as follows: In this study, we report the co-crystallographic analyses of AsDMS, an enzyme that converts substrate 1 into product 2, and the biochemical characterization of site-specific variants. During the preparation of this manuscript, Osika et al.1 disclosed the structure of AsDMS in complex with a non-physiological ligand. In this report, we obtained co-crystal structures of the AsDMS-1 and AsDMS-3 complexes. The obtained co-crystal structures of AsDMS represent the first experimentally determined physiological substrate-bound structures of a HAD-TCβ enzyme, revealing distinct substrate-binding pockets for the HAD and TCβ domains.
The co-crystal structures reported in this study involve the physiological substrate, whereas the physiological substrate-free structure of AsDMS was independently reported contemporaneously by Osika et al.,1 highlighting the complementary nature of these studies. Based on 18O-labelling, MESG assays, and the substrate-free crystal structure, Osika et al.1 proposed a mechanism that releases Pi in a stepwise manner. In the present study, we elucidate the catalytic mechanism (Fig. 6) through co-crystal structures with the physiological substrates and comprehensive site-directed mutagenesis analyses, providing firm experimental evidence for the catalytic process.
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
References
- K. R. Osika, M. N. Gaynes and D. W. Christianson, Proc. Natl. Acad. Sci. U. S. A., 2025, 122(26), e2506584122 CrossRef CAS PubMed.
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