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. 2018 Jan 29;8:1776. doi: 10.1038/s41598-018-19920-y

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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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Key residues highlighted on the crystal structure model of CysE and CysM proteins. Cartoon diagram of the trimer (A) E. coli serine acetyltransferase protein (CysE, PDB ID: 1T3D) and dimer (B) E. coli O-acetylserine sulfhydrylase (CysM, PDB ID: 2BHS) are shown in gray scheme with each monomer in different exposure. The active site residues (red), substituted cysteine (yellow) and methionine (blue or purple) residues are highlighted in the left diagram. Methionines displayed in purple participate as an active site residue while methionines in blue are not part of the active site. Panels on the right represent the active center (top), the two closest cysteines (middle), and an example of methionine-aromatic motifs (bottom) found within the protein structures of CysE and CysM. Distances between each amino acid residue are denoted in angstroms.