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. 2019 Jan 29;9:825. doi: 10.1038/s41598-018-36069-w

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© The Author(s) 2019

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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Alignment of the Loop 1 regions in L1 GUS enzymes. (a) Overlay of EcGUS (3LPG; dark green) with SaGUS (4JKK; yellow), CpGUS (4JKM; indigo), FpGUS (cyan), and LrGUS (magenta), with pNPG shown docked into the active site of EcGUS. (b) Overlay of EcGUS and EeGUS (purple). The canonical Loop 1 is shown in dark purple. The additional active site proximal loop, termed “Ee Extra Loop”, is shown in magenta. Residues G152 through G156 were not previously built and are not shown. (c) Overlay of EcGUS and RgGUS (dark pink) (d) Sequence alignment of the Loop 1 regions from the seven L1 GUS enzymes characterized in this study. Amino acids that form the alpha helix in the Loop 1 of RgGUS are boxed in red. Amino acids that correspond to the alpha helix position in the Loop 1 of RgGUS are underlined.