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. 2018 Aug 20;9:1942. doi: 10.3389/fmicb.2018.01942

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Copyright © 2018 Golkar, Zieliński and Berghuis.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Homology model of EreA based on the structure of BcR135. (A) The model is depicted, highlighting secondary structure elements. The colors used illustrate sequence conservation within the five Ere enzymes, with dark blue indicating completely conserved residues, light blue residues that are conserved among only 3–4 members, and white residues that are not conserved. (B) The enzyme is rotated and shown in surface representation, highlighting the putative active site and the location of putative catalytic residues. The figure was prepared using PyMOL (Schrödinger, 2017).