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. 2022 Jun 16;13:891610. doi: 10.3389/fmicb.2022.891610

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Copyright © 2022 Hopf, Roth, de Souza, Galina, Czeczot, Machado, Basso and Bizarro.

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(s) 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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FabK structure. (A) Structure of Streptococcus pneumoniae FabK (SpFabK, PDB: 2Z6I). The LID and the TIM barrel fold are indicated. The latter, together with a bound flavin mononucleotide (FMN) cofactor, are represented in more detail. (B) Superposition of Porphyromonas gingivalis FabK (PgFabK, PDB: 4IQL, represented in pink) with Thermotoga maritima FabK (TmFabK, PDB: 5GVH, represented in cyan) and S. pneumoniae FabK (SpFabK, PDB: 2Z6I, represented in purple). (C) Superposition of SpFabK bound to FMN cofactor (PDB: 2Z6I) with the ternary structure of SpFabK bound to FMN and a phenylimidazole derivative inhibitor (compound 1; PDB: 2Z6J). The orientation of a putative catalytic histidine residue (H144) rotates upon inhibitor binding. The superposition of structures was performed using the Matchmaker tool from UCSF ChimeraX. Created with UCSF ChimeraX (Pettersen et al., 2021) and BioRender.com.