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. 2018 Jun 20;8:186. doi: 10.3389/fcimb.2018.00186

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Copyright © 2018 Ayana, Yadav, Kumari, Ramu, Garg, Pati and Singh.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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(A) Docking study of LdPAT4 with palmitoylation inhibitor 2-BMP. (i) The protein accessible surface area was visualized for flexible ligand docking. (ii) Strong H-bonding indicated key residues involved in the interaction of the catalytic domain of LdPAT4 to 2-BMP. (B) Immunofluorescence analysis demonstrating expression and cellular localization of LdPAT4 in Leishmania promastigotes. Scale bar in white indicates 5 μM. (C) (i) Normaski and fluorescence images showing the catalytic activity of LdPAT4-DHHC using click chemistry in transformed E. coli cells. Scale bar in white indicates 2 μM. (ii) Fluorometer readings showing uninduced, induced and 2-BMP treated LdPAT4-DHHC expressing E. coli cells (**p < < 0.05). Data are represented as mean ± SEM.