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Figure 3
Structural comparison of the N-terminal domain (NTD) and C-terminal domain (CTD) of DynU16 with similar folds encompassing diverse functionalities including cyclization, aromatization and isomerization. The DynU16 helix-grip fold shares distant structural homology to the START di-domain polyketide-biosynthesis cyclase StfQ (PDB entry 4xrt; Caldara-Festin et al., 2015BB6) and aromatase BexL (PDB entry 4xrw; Caldara-Festin et al., 2015BB6). Additionally, the helix-grip fold resembles enzymes in the NTF2-domain family, including SnoaL, a mono-domain cyclase (PDB entry 1sjw; Sultana et al., 2004BB30), and TsrD, a mono-domain isomerase (PDB entry 5x7l; Y. Song, Z. Lin, W. Deng & W. Liu, unpublished work). The catalytic domains selected for illustration are marked with an asterisk. The figure was generated with PyMOL (version 2.4.1; Schrödinger).

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 77| Part 10| October 2021| Pages 328-333
https://doi.org/10.1107/S2053230X21008943
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