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. 2016 Sep 21;14:81. doi: 10.1186/s12915-016-0303-0

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© Stojanoski et al. 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 2 — Structure of the catalytic domain of MCR-1 phosphoethanolamine transferase. Secondary structure elements are depicted as a ribbon model and colored in cyan (helices), purple (strands), and salmon (loops). Additionally, the phosphothreonine 285 is represented in sticks. Right, rotated 90 °, a view of the characteristic alkaline phosphatase α/β/α fold of cMCR-1