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. 2017 Dec 6;8:1965. doi: 10.1038/s41467-017-01975-6

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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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Fig. 2 — Biosynthesis of hydroxamate metalloproteinase inhibitors. a Organization of the mat and the act biosynthetic gene cluster from A. atramentaria DSM 43919 and Streptomyces sp. ATCC 14903 (NCIMB 8845), respectively. b Biosynthetic model for the assembly and modification of the matlystatins. A adenylation domain, ACP acyl carrier protein, AT acyl-transferase domain, C condensation domain, KS ketosynthase, PCP peptidyl carrier protein, TE thioesterase