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. 2017 Jul 13;7:5312. doi: 10.1038/s41598-017-05509-4

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© The Author(s) 2017

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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A model of PhaC activation in dimeric form. (a) The closed form as observed in our PhaC_Cs-CAT structure. The N domain is proposed to contribute to stabilization of the dimer. (b) The partially open form as observed in the PhaC_Cn-CAT structure. The structure provides a possible path to the active site, but no apparent path for product. (c) The single active site provides a full active site architecture for initiation of acylation and chain elongation. (d) The Cys-bound product in one protomer attacks the 3HB-Cys thioester of the other protomer in the dimer for chain elongation.