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. 2019 May 16;9:7482. doi: 10.1038/s41598-019-44013-9

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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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Wild type and mutant’s interactions with POA. (A) MTB RpsA WT and MT secondary structure. Mutation site has been pointed, where the conversion of loop into helix and sheet into coil, encircled in D342N, D343N, A344P, and I351F. (B) WT formed two H-bonds with two POA molecules. MT had fewer hydrogen as compared to WT.