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. 2019 Apr 12;9:5965. doi: 10.1038/s41598-019-42435-z

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© The Author(s) 2019

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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Binding of mature lysostaphin to pentaglycine. Two molecules in the asymmetric unit of the mature lysostahin (PDB:4LXC) were superimposed to show the flexibility of the domains. The catalytic domains (yellow and gray) differ in orientation by almost 100°. Catalytic zinc ion shown as a ball and SH3b domains are green. Moreover, the structure of mature lysostaphin was superimposed with ligands from complex structures of LytM catalytic domain with substrate analogue (PDB:4ZYB) and LssSH3b domain with pentaglycine (PDB:5LEO).