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. 2016 Jul 8;9:140. doi: 10.1186/s13068-016-0550-x

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© The Author(s) 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 4 — Modeled structures of THSAbf. a The overall two domain structure composed of a (β/α)₈ folded catalytic domain and a C-terminal domain displaying β-sandwich architecture. Two structural conformers of THSAbf (open gray and violet, closed yellow and pink) are superposed and the β2α2 loop in two different positions is encircled. b Zoom on the catalytic site of the two modeled THSAbf conformers (gray and yellow) and that of GsAbf (1QW8, green). The side chains of the two catalytic residues (Glu 177 and 296 in THSAbf) are shown as sticks. (Figure prepared using PyMOL™ Molecular Graphics System, Version 1.7.2.1)