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. 2020 Dec 4;11:6204. doi: 10.1038/s41467-020-20044-z

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© The Author(s) 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — a Structure of AlfC with active-site annotated. b Structure of closest homolog α-L-f1wt, exhibiting a C-terminal domain present in most α-fucosidases, but absent in AlfC. c Tetrameric assembly of AlfC compared to d α-l-f1wt (hexamer) and e Tmα-fuc (hexamer). Active-site separation is measured by the distance between catalytic nucleophiles. f Structure of AlfC active site with l-fucose bound. Enzyme contacts are shown by dashed lines. The catalytic nucleophile is shown in blue, while lead candidates for the general acid/base are shown in yellow. A mobile loop containing D242 is annotated. g Cartoon representation of AlfC structure colored by B-factor, highlighting high B-factors in the mobile loop that precedes a disordered region.