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. 2018 Nov 6;8:16372. doi: 10.1038/s41598-018-34678-z

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© The Author(s) 2018

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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Loop 3 (or the α2-helix loop) and loop 5 are important for the substrate preferences of the GUSs. Comparison of the ABSs of the five bacterial GUSs. The structures of RgGUS/UIFG (b), 4JKM (CpGUS-apo) (c), 3LPG (the EcGUS/N-substituted-thiourea derivative) (d), and BfGUS/UIFG (e) were superimposed on the structure of BifdGUS^E479A/10 (a). The substrate-binding sites of GUSs are located at the center of the TIM barrel domains. Panels (a–e) display the ABSs that are formed by the conserved loop 6 (L6) and variable loop 5 (L5) and loop 3 (L3) or α2-helix loop. The α2-helix loop in BifdGUS occupies a position similar to that of loop 3 in the other GUSs. (f) Sequences of loop 3 (or the α2-helix loop) and loop 5 in the five bacterial GUSs. Residues interacting with the aglycone of 10 are shown as blue, cyan, magenta, yellow, and olive sticks in panels a–e, respectively. (g) Molecular structure of 10.