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. 2023 Mar 23;14:1624. doi: 10.1038/s41467-023-37287-1

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© The Author(s) 2023

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. 4 — a Proposed interaction model for MpaA, MpaB, and MpaC. The RRE domain (dark grey) of MpaB interacts with the conserved leader region of MpaA. The C-terminus (depicted as “-OH”) of MpaA is directed into the active site of MpaC for modification. b Summary of MpaA variant processing upon E. coli co-expression with MpaB/C. c Mass spectra of MpaA after co-expression with MpaC, and MpaB or MpaB_1-266. The RRE domain of MpaB is dark grey. d The structure of MpaA1-MpaB-MpaC predicted using AlphaFold-Multimer⁴⁰. MpaA1, MpaB, and MpaC are shown as cartoons in green, orange, and blue, respectively. The positioning of cofactor NADP was imported using a homologous alcohol dehydrogenase (PDB ID: 6C76) as a template. e, View of the leader peptide-RRE domain binding interface⁴⁰. Select residues of MpaA and MpaB are in green and orange, respectively. f View of the C-terminal Thr24 of MpaA in the substrate-binding pocket of MpaC.