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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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PhaC_Cs-CAT forms a dimer in the crystal. (a) A top-view of the PhaC_Cs-CAT dimer along the pseudo-dyad axis. The color codes of mol B are the same as in Fig. 1, with mol A core (gray) and CAP (yellow) subdomains shown. The distance between the catalytic cysteine residues is 28.1 Å (red double-headed arrow). (b) As in a, but the side-view. Contact areas I (red) and II (orange) are indicated by broken circles. The N-termini of both protomers are located at the same side of the dimer. (c) Contact area I forms a hydrophobic cluster with nonpolar residues from ηB’-αC loop (Leu369, Trp371) and αC helix (Pro386, Phe387, Phe390) from both protomers. The segment (Asn372-Thr383) between ηB’-αC loop (Leu369, Trp371) and αC helix are disordered in our crystal (dashed lines). (d) Contact area II contains salt bridges (Arg365–Glu329) buried inside the interface formed by nonpolar residues of ηA helix (Phe332, Phe333) and β8-α4 loop (His448, Leu451) from both protomers. Hydrogen bonds are indicated by broken lines.