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. 2015 Sep 15;6(5):e02327-14. doi: 10.1128/mBio.02327-14

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Copyright © 2015 Xu et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited.

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FIG 3 — Structure comparisons of a prototypic NlpC/P60 domain and SH3b-NlpC/P60 fusion proteins (DvLysin, AvPCP, BoYkfC, and BcYkfC). (A) Tree representation of relationships based on structural similarity. (B) Superimposed structures. Equivalent residues are colored by domain (magenta, SH3b1; orange, SH3b2; green, NlpC/P60), while nonsuperimposed residues are shown in gray, except that the c-clip domain of DvLysin is in blue. The Cα atoms of catalytic cysteines are shown as green spheres. (C) Side-by-side comparison of the domain architecture of lysins and cell wall recycling enzymes.