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. 2023 Jul 6;2(7):pgad221. doi: 10.1093/pnasnexus/pgad221

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© The Author(s) 2023. Published by Oxford University Press on behalf of National Academy of Sciences.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Fig. 1. — WUR7 decarboxylases WUR7_ADC1 and WUR7_ADC2 were aligned with the TDC ZP_02040762 from R. gnavus, to highlight key residues conferring Trp specificity according to the model proposed by Williams et al (11) which are indicated by the black star over the residue. A) Fragments of WUR7_ADC1 share high similarity (approximately 70% identity) with ZP_02040762. Proteins are numbered according to ZP_02040762. *Significance of BlastP alignments using ZP_02040762 as query and WUR7_ADC1 and WUR7_ADC2 as subjects; values are calculated over the entire amino acid sequence. B) Overall superimposition of WUR7_ADC1 (red and orange chains) on chains B (blue) and D (cyan) of ZP_02040762 crystal. C) 3D positioning of superimposed residues directly interacting with the indole-based inhibitor PLP-(S)-alpha-FMT ketone (yellow).