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. 2018 Jun 19;8:198. doi: 10.3389/fcimb.2018.00198

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Copyright © 2018 Lyles and Eichenbaum.

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 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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Overall structure of proteins with HemS motifs. (A) Represents ChuS, (B) Represents HemS, and (C) Represents PhuS. In all representations the N-terminal HemS domain is in white and the C-terminal HemS domain is in blue. Looking at the structure, ChuS consists of a mix of α-helices and β-strands arranged so that the β-sheets form the core of the enzyme and are flanked by three α-helices on one side and two on the other side. This configuration is conserved in the structure of HemS, although HemS is symmetrical, with three α-helices on each side.